|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-768 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1324.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEptsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGktEA 578
Cdd:cd01377 398 EQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKS--EA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 579 HFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSgaQAGEGGGGKKGGKKKGSSFQTVSALFRENLN 658
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFK--DYEESGGGGGKKKKKGGSFRTVSQLHKEQLN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 659 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFi 738
Cdd:cd01377 554 KLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD- 632
|
650 660 670
....*....|....*....|....*....|
gi 826320982 739 DSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd01377 633 DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 1313.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDS--KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG-AQAGEGGGGKKGGKKKGSSFQTVSALFRENLN 658
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATfATADADSGKKKVAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 659 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 738
Cdd:cd14913 559 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 826320982 739 DSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14913 639 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 1311.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQA--GEGGGGKKGGKKKGSSFQTVSALFRENL 657
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTaeAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 658 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 737
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 826320982 738 IDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 1288.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGGG--GKKGGKKKGSSFQTVSALFRENL 657
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEggGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 658 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 737
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 826320982 738 IDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1255.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEptSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG-AQAGEGGGGKKGGKKKGSSFQTVSALFRENLN 658
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTyASAEADSGAKKGAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 659 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 738
Cdd:cd14918 559 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 826320982 739 DSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14918 639 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 1244.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGG----GGKKGGKKKGSSFQTVSALFRE 655
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGAsaggGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 656 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 735
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 826320982 736 QFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 1231.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEpTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQ-QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFS---GAQAGEGGGGKKGGKKKGSSFQTVSALFREN 656
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyaGAEAGDSGGSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 657 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 736
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 826320982 737 FIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14923 640 FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-768 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 1167.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGE--KKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 419 TVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 499 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKG-KTE 577
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKrKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 578 AHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLF----SGAQAGEGGGGKKGGKKKGSSFQTVSALF 653
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYenyvGSDSTEDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 654 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 733
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 826320982 734 EGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1139.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG-AQAGEGGGGKKGGKKKGSSFQTVSALFRENLN 658
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANyAGADAPIEKGKGKAKKGSSFQTVSALHRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 659 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 738
Cdd:cd14917 559 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 826320982 739 DSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14917 639 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1137.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEpTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKE-NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFS---GAQAGEgGGGKKGGKKKGSSFQTVSALFREN 656
Cdd:cd14916 480 FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyaSADTGD-SGKGKGGKKKGSSFQTVSALHREN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 657 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 736
Cdd:cd14916 559 LNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 638
|
650 660 670
....*....|....*....|....*....|..
gi 826320982 737 FIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14916 639 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-768 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1040.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 88 IEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEeptsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 248 GKFIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLItTNPYDYAFVSQ-GEITVPSI 326
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 327 DDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPR 406
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 407 VKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 486 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSN 564
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 565 NFQKPKPtkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGGGGKKGGKKK-- 642
Cdd:pfam00063 470 HFQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpk 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 643 ---GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 719
Cdd:pfam00063 547 rtkKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 826320982 720 FKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:pfam00063 627 FVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 1038.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEeptsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKpELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAH 579
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLF-------SGAQAGEggggkkGGKKKGSSFQTVSAL 652
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFenyistdSAIQFGE------KKRKKGASFQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 653 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 732
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 826320982 733 PEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-780 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 997.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 81 NPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkeepTSGKMQGTLEDQIISANPLLEAFGNAKTVR 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS----------GSNTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 241 NDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTnPYDYAFVSQG- 319
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 320 EITVPSIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKAAYLTSLNSADL 398
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 399 LKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 478
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYd 557
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 558 QHLGKSNNFQKPKPtkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGaqageggggKK 637
Cdd:smart00242 468 QHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS---------GV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 638 GGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 717
Cdd:smart00242 536 SNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPF 615
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 718 ADFKQRYKVLNASAIPEGQFiDSKKASEKLLGSIDVDHTQYKFGHTKVFFKAGLLGTLEEMRD 780
Cdd:smart00242 616 DEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-768 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 996.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEptsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQSSDG------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAVD 340
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 341 ILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQTV 420
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 421 QQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 501 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGK-TEAH 579
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 580 FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSgaqaGEGGGGKKGGKKKGSSFQTVSALFRENLNK 659
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK----EEEAPAGSKKQKRGSSFMTVSNFYREQLNK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 660 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFID 739
Cdd:cd14934 552 LMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVD 630
|
650 660
....*....|....*....|....*....
gi 826320982 740 SKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14934 631 NKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 980.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEptsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAA----KSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTK-GKTEA 578
Cdd:cd14909 397 EQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 579 HFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFS--GAQAGEGGGGKKGGKKKGSSFQTVSALFREN 656
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAdhAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 657 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 736
Cdd:cd14909 557 LNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE 636
|
650 660 670
....*....|....*....|....*....|..
gi 826320982 737 fiDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14909 637 --DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-768 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 839.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFATIAvtgekKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-----GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDY----AFVSQGEITVPSIDDQEELMA 334
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYylndYLNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 335 TDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNE 412
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 413 FVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 490
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 491 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP 569
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 570 KptkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSmktlallfsgaqageggggkkggkkkgssfqtv 649
Cdd:cd00124 475 R----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS--------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 650 saLFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 729
Cdd:cd00124 518 --QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595
|
650 660 670
....*....|....*....|....*....|....*....
gi 826320982 730 SAiPEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd00124 596 GA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1116 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 828.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 30 KPFDAKTSVFVADPKESFVKATVqsreggKVTAKTEGGSTVTVK--DDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLK 107
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKV------TEEGKKEDGESVSVKkkVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 108 ERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTV 187
Cdd:COG5022 88 KRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 188 NTKRVIQYFAtiAVTGekkkeepTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIE 267
Cdd:COG5022 168 NAKRIMQYLA--SVTS-------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 268 TYLLEKSRVTFQLQAERSYHIFYQIMSNKkPELIEMLLITTNPYDYAFVSQGE-ITVPSIDDQEELMATDSAVDILGFTA 346
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 347 DEKVAIYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQTVQQVYNA 426
Cdd:COG5022 318 EEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 427 VGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKK 506
Cdd:COG5022 397 RDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 507 EGIEWEFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKSNNFQKPKPTKGKteahFSLV 583
Cdd:COG5022 477 EGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 584 HYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEggggkkggkkKGSSFQTVSALFRENLNKLMTN 663
Cdd:COG5022 552 HYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE----------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 664 LRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI---DS 740
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 741 KKASEKLLGSIDVDHTQYKFGHTKVFFKAGLLGTLEEMRDEKLAQLITRTQAICRGYLMRVEFRKMMERRESIFCIQYNI 820
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 821 RAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKAKEELaKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSL 900
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKR 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 901 ADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEKHATEN 975
Cdd:COG5022 861 FSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLLNN 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 976 -KVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQekklRMDLERAK 1054
Cdd:COG5022 940 iDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGALQEST 1015
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 826320982 1055 RKLEGDLKLAQESTMDIENDKQQLDEKLKKKefEMSNLQSKIEDEQavgMQLQKKIKELQAR 1116
Cdd:COG5022 1016 KQLKELPVEVAELQSASKIISSESTELSILK--PLQKLKGLLLLEN---NQLQARYKALKLR 1072
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-768 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 786.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKK-----KEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 256 GATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMAT 335
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 336 DSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEFV 414
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 415 TKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 494 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgksNNFQKPKPTK 573
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH----SMHPKFMKTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 574 GKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGGGGKKGGKKKGSS-----FQT 648
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARtrkgmFRT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 649 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 728
Cdd:cd14911 556 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 635
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 826320982 729 ASAIPEGqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14911 636 PNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-768 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 768.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEeptsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKD----HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 419 TVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 497 FVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKPTK 573
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 574 GktEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLF---------SGAQAGEGGGGKKGGKKKGS 644
Cdd:cd14920 473 D--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivglDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 645 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 724
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 826320982 725 KVLNASAIPEGqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14920 631 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-768 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 720.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAVD 340
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL-EDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 341 ILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 499 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKptKGK 575
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 576 TEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQ--------AGEGGGGKKGGKKKGSSFQ 647
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrivgldkvAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 648 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 727
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 826320982 728 NASAIPEGqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14932 637 TPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-768 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 693.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAVD 340
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 341 ILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 499 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPTKGK 575
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 576 TEahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQ--AGEGGGGKKGGKKKGSS-------F 646
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDriVGLDQMAKMTESSLPSAsktkkgmF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 647 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 726
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 826320982 727 LNASAIPEGqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-768 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 685.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFATiaVTGEKKKEepTSgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGGSSSGE--TQ------VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 419 TVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 497 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNN-FQKPKPTKGK 575
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 576 teahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKtlallfsgaqageggggkkggkkkgssFQTVSALFRE 655
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR---------------------------KKTVGSQFRD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 656 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAipEG 735
Cdd:cd01380 519 SLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--EW 596
|
650 660 670
....*....|....*....|....*....|...
gi 826320982 736 QFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd01380 597 LRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-768 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 671.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAVD 340
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 341 ILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQTV 420
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 421 QQVYNAVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKptKGKT 576
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 577 EAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA-------QAGEGGGGKKGGKKKGSSFQTV 649
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdrivgldKVSGMSEMPGAFKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 650 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 729
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 826320982 730 SAIPEGqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd15896 638 NAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-768 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 667.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEeptsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 419 TVQQVYNAVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14919 312 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 498 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPTKG 574
Cdd:cd14919 392 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 575 KteAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQ--------AG-EGGGGKKGGKKKGSS 645
Cdd:cd14919 471 K--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvAGmSETALPGAFKTRKGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 646 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14919 549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 826320982 726 VLNASAIPEGqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14919 629 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-768 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 652.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAVD 340
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 341 ILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNAVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 498 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKPTkg 574
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHL-- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 575 KTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA-------QAGEGGGGKKGGKKKGSSFQ 647
Cdd:cd14930 471 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegivgleQVSSLGDGPPGGRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 648 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 727
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 826320982 728 NASAIPEGqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14930 631 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-768 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 634.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGekkkeeptsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGS-------------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSA 338
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 419 TVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 498 VLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFqkpkptKGKT 576
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 577 EAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKtLALLFSGAQAGEGGGGKKGGKKKGSSF--QTVSALFR 654
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFASKMLDASRKALPLTKASGSDSqkQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 655 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 734
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSA 615
|
650 660 670
....*....|....*....|....*....|....
gi 826320982 735 GQFIDSkkASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd01383 616 SQDPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-768 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 632.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIavtgekkkeeptSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAV 339
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKG 417
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 418 QTVQQVYNAVGALAKAIYEKMFLWMVTRIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 494 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPkpt 572
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 573 KGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFsgaqagegGGGKKGGKKKGSSFQTVSAL 652
Cdd:cd01381 462 KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF--------NEDISMGSETRKKSPTLSSQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 653 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnASAI 732
Cdd:cd01381 534 FRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VPGI 612
|
650 660 670
....*....|....*....|....*....|....*.
gi 826320982 733 PEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd01381 613 PPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-768 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 626.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFAtiAVTGekkkeePTSGKMQGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIA--AVSG------GSESEVERV-KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAVD 340
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 341 ILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKAAYLTSLNSADLLKALCYPRVKVGNEF---VTKG 417
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 418 QTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHhm 496
Cdd:cd01378 312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 497 FVL--EQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyDQHLGKSNNFQKPKPT 572
Cdd:cd01378 390 LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 573 KGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFsgaqageggggkKGGKKKGSSFQ--TVS 650
Cdd:cd01378 468 FELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF------------PEGVDLDSKKRppTAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 651 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 730
Cdd:cd01378 536 TKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPK 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 826320982 731 AIPEGQFIDsKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd01378 616 TWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-768 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 608.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFAtiAVTGEkkkeeptsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN-----------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKK--PELIEmLLITTNPYDYAFVSQ-GEITVPSIDDQEELMATDS 337
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 338 AVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTK 416
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 417 GQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 497 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKPTKGK 575
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 576 TEahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFS------GAQAGEGGGGKKGGKKKGSSFQTV 649
Cdd:cd14883 466 TE--FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdllaLTGLSISLGGDTTSRGTSKGKPTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 650 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 729
Cdd:cd14883 544 GDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 826320982 730 SAIPEGQFIDsKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14883 624 RARSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-768 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 583.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFATIAvtgekkKEEPTSGKmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDS 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 338 AVDILGFTADEKVAIYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADKAAYLTSLNSADLL--------KALCYPRVKV 409
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEFHLKAAAELLmcdekaleDALCKRVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 410 GNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd01384 306 PDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 490 QFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQK 568
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 569 PKptkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEggggkkggKKKGSSFQT 648
Cdd:cd01384 464 PK----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREG--------TSSSSKFSS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 649 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLn 728
Cdd:cd01384 532 IGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL- 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 826320982 729 ASAIPEGQFiDSKKASEKLLGSIDVDhtQYKFGHTKVFFK 768
Cdd:cd01384 611 APEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-768 |
1.15e-172 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 540.90 E-value: 1.15e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 176 LITGESGAGKTVNTKRVIQYFATI----AVTGEKKKEEPTSGKMQ--GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfAQGASGEGEAASEAIEQtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTnPYDYAFVSQGEITVPSIDDQ 329
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 330 EELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKAAYLTSLNSADLLKALCYPRVK 408
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 409 VGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 489 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYDQHLGK 562
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 563 SN------------NFQKPKPTKGKteaHFSLVHYAGTVDYNINGWLDKNKDPLNEtvvglyqksSMKTLallfsGAQAG 630
Cdd:cd14890 479 SGsggtrrgssqhpHFVHPKFDADK---QFGIKHYAGDVIYDASGFNEKNNETLNA---------EMKEL-----IKQSR 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 631 EGGGGKkggkkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 710
Cdd:cd14890 542 RSIREV-----------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQG 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 711 FPSRILYADFKQRYKVLNASAipegqfiDSKKASEKLLGSI-DVDHTQYKFGHTKVFFK 768
Cdd:cd14890 611 FALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-768 |
3.68e-172 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 539.14 E-value: 3.68e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 182 GAGKTVNTKRVIQYFATIAvtgekkkeeptsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd01382 84 GAGKTESTKYILRYLTESW------------GSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 262 ASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLittnpydyafvsqgeiTVPSIDDQEELMATDSAVDI 341
Cdd:cd01382 152 VGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 342 LGFTADEKVAIYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------AAYLTSLNSADLLKALCYpRVKVGNE 412
Cdd:cd01382 216 IGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 413 FVTKGQ------TVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 487 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLgksNN 565
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---NH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 566 FQKPKPTKGKTEAH--------FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFsgaQAGEGGGGKK 637
Cdd:cd01382 445 FRLSIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF---ESSTNNNKDS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 638 GGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 717
Cdd:cd01382 522 KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 826320982 718 ADFKQRYKVLNASAIPEgqfIDSK---KASEKLLGSIDVDhtqYKFGHTKVFFK 768
Cdd:cd01382 602 HDLYNMYKKYLPPKLAR---LDPRlfcKALFKALGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-768 |
9.75e-167 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 525.03 E-value: 9.75e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFATIAVTGEKKKEeptsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF--- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 256 ------GATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMS-----------------------NKKPELIEMLLI 306
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 307 TT-NPYDYAFVSqGEITVPSIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTE 382
Cdd:cd14888 231 EPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 383 VADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIG 461
Cdd:cd14888 310 DLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 462 VLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELI-EKPMGIFSILEEE 540
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 541 CMFPKATDTSFKNKLYDQHLGkSNNFQKPKptkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTL 620
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKHKG-HKRFDVVK----TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFI 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 621 ALLFSgaqagEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGV 700
Cdd:cd14888 544 SNLFS-----AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGV 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 701 LEGIRICRKGFPSRILYADFKQRYKVLnasAIPEGQfidskkasekllgsidVDHTQYKFGHTKVFFK 768
Cdd:cd14888 619 LQAVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1925 |
1.00e-166 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 539.38 E-value: 1.00e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 848 EKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATER 927
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 928 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQ 1007
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1008 TLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEF 1087
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1088 EMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK 1167
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1168 KREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNF 1247
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1248 EKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKA 1327
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1328 KNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiHRTEELEEAKKKLAQRLQDAEEHVE 1407
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1408 AVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWK-----HKYEETQAELEASQKESRSLSte 1482
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKaisarYAEERDRAEAEAREKETRALS-- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1483 lfkVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILR 1562
Cdd:pfam01576 641 ---LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1563 IQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAI 1642
Cdd:pfam01576 718 LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1643 RNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQN 1722
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1723 TSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEA 1802
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1803 EQLALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKR 1882
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 826320982 1883 QAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVK 1925
Cdd:pfam01576 1038 QLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-768 |
2.04e-164 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 518.56 E-value: 2.04e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeeptSGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELiEMLLITTNPYDYAFvSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTK 416
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 417 GQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 497 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKgkt 576
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 577 eAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFS------GAQAGEGGGGKKGGKKKGSSFQTVS 650
Cdd:cd14903 463 -TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKekvespAAASTSLARGARRRRGGALTTTTVG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 651 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnas 730
Cdd:cd14903 542 TQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF--- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 826320982 731 aIPEGQFIDSKKAS--EKLLGSIDVDH-TQYKFGHTKVFFK 768
Cdd:cd14903 619 -LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-768 |
1.52e-163 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 515.48 E-value: 1.52e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTgekkkeepTSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS--------TNG-----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSnkKPELIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMATDSA 338
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLTSLNSADLLKALCYPRVKVgnefvt 415
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanrDVLKEVATLLGVDAATLEEALTSRLMEI------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 416 KGQ-------TVQQVYNAVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14872 299 KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 488 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSnnF 566
Cdd:cd14872 379 LQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--T 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 567 QKPKPTKGkTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEggggkkggkkkGSSF 646
Cdd:cd14872 456 FVYAEVRT-SRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQ-----------KTSK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 647 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 726
Cdd:cd14872 524 VTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRF 603
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 826320982 727 LNaSAIPEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14872 604 LV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-768 |
1.30e-161 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 511.92 E-value: 1.30e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 183 AGKTVNTKRVIQYFATIavtgekkkeeptSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd01385 84 SGKTESTNFLLHHLTAL------------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 262 ASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAVD 340
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 341 ILGFTADEKVAIYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 419 TVQQVYNAVGALAKAIYEKMFLWMVTRINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 495 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKlYDQHLGKSNNFQKPKptk 573
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 574 gKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSM--------------KTLALL-------FSGAQAGEG 632
Cdd:cd01385 466 -VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavFRWAVLrafframAAFREAGRR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 633 GGGKKGGKKKGSSF---------------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRC 697
Cdd:cd01385 545 RAQRTAGHSLTLHDrttksllhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRY 624
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 698 NGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEGQfIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-768 |
8.66e-159 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 502.19 E-value: 8.66e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIavtgekkkeeptsGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL-------------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIM----SNKKpeLIEMLLITTNPYDYAFVSQGEITVPSIDD--QEEL 332
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 333 MATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKAAYLTSLNSADLLKALCYPRVK 408
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 409 VGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 486 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 560
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 561 gKSNNFQKPKptkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLAllfsgaqageggggkkggk 640
Cdd:cd01379 460 -KSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 641 kkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 720
Cdd:cd01379 516 ------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADF 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 826320982 721 KQRYKVL--NASAIPEGqfidSKKASEKLLGSIDVDHtqYKFGHTKVFFK 768
Cdd:cd01379 590 LKRYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-766 |
9.23e-159 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 502.78 E-value: 9.23e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 172 --NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKKEEptSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLA--SVSSATTHGQ--NATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNP-YDYAFVSQGEITVPSIDD 328
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 329 QEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY-LTSLNSADLLKALCYPRV 407
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 408 KVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 486 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSN 564
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 565 NFQKPKPTKGKteAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLAllfsgaqageggggkkggkkkgs 644
Cdd:cd14901 475 SFSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 645 sfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 724
Cdd:cd14901 530 --STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTY 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 826320982 725 KVLNASAIPEGQFIDSKKASEKLLGSIDV----DHTQYKFGHTKVF 766
Cdd:cd14901 608 SCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-768 |
2.11e-158 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 501.98 E-value: 2.11e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEptsgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgATGK 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNLVTE------------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQI---MSNKKPELIEMLlittNPYDYAFVSQG-EITVPSIDDQEELMATD 336
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELlagLPAQLRQKYGLQ----EAEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 337 SAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADKA-----AYLTSLNSADLLKALCYPRVKVGN 411
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTETRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 412 EFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 491
Cdd:cd01387 303 ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 492 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPK 570
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 571 ptkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAgegGGGKKGGKKKGSSF---- 646
Cdd:cd01387 461 ----MPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRA---QTDKAPPRLGKGRFvtmk 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 647 ---QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 723
Cdd:cd01387 534 prtPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDR 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 826320982 724 YKVLNASAIPEGQFIDSKKA-SEKLLGSIDVDhtQYKFGHTKVFFK 768
Cdd:cd01387 614 YRCLVALKLPRPAPGDMCVSlLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-768 |
1.03e-157 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 500.06 E-value: 1.03e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRG--KKRQEAPPHIFSISDNAYQFMLTDR----ENQSILIT 178
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKpELIEMLLITTNPYDYAFVSQGE-ITVPSIDDQEELMATDS 337
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 338 AVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KAAYLTSLNSADLLKALCYpRVKVGnefvT 415
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST----A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 416 KGQ------TVQQVYNAVGALAKAIYEKMFLWMVTRIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSLEQL 479
Cdd:cd14892 321 RGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSFEQL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 480 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNKLYD 557
Cdd:cd14892 401 CINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIYHQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 558 QHLGKSNNFQKPKptkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMktlallfsgaqageggggkk 637
Cdd:cd14892 480 THLDKHPHYAKPR----FECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 638 ggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 717
Cdd:cd14892 536 ---------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQF 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 718 ADFKQRYKVL-------NASAIPEGQFIDSKKASEKLLGSIDVDHTQykFGHTKVFFK 768
Cdd:cd14892 601 EEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-768 |
9.12e-154 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 488.92 E-value: 9.12e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAvtgeKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVIS----QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTnPYDYAFVSQ-GEITVPSIDDQEELMATDSA 338
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILGFTADEKVAIYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADK-----AAYLTSLNSADLLKALCYPRVKVGNEF 413
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 414 VTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 494 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgkSNNfqkPKPTK 573
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANN---HFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 574 GKTEAH-FSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLF---SGAQAGEGGGGKKGGKKkgssfQTV 649
Cdd:cd14873 461 PRVAVNnFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFehvSSRNNQDTLKCGSKHRR-----PTV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 650 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL-N 728
Cdd:cd14873 536 SSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 826320982 729 ASAIPEgqfiDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14873 616 NLALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-768 |
4.28e-147 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 469.94 E-value: 4.28e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIavtgekkkeeptSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLItTNPYDYAFVSQGEITVPSIDDQEEL-----MAT 335
Cdd:cd14897 151 LLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 336 DSaVDIL---GFTADEKVAIYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADK-----AAYLTSLNSADLLKALCYPRV 407
Cdd:cd14897 230 DL-TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 408 KVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCIN 482
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDqHLG 561
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 562 KSNNFQKPKptKGKTEahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFsgaqageggggkkggkk 641
Cdd:cd14897 462 ESPRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 642 kgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 721
Cdd:cd14897 521 --------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 826320982 722 QRYKVL-----NASAIPEGQFIDSKKasekllgsiDVDHTQYKFGHTKVFFK 768
Cdd:cd14897 593 KRYKEIcdfsnKVRSDDLGKCQKILK---------TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-768 |
7.14e-145 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 465.27 E-value: 7.14e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 173 QSILITGESGAGKTVNTKRVIQYFATIAvTGEKKKEEPT--------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLS-QQEQNSEEVLtltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 245 SRFGKFIRIHFG-ATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNP--YDYAFVSQGE- 320
Cdd:cd14907 162 SRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNc 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 321 ITVPSIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLTSLNSADL 398
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 399 LKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQL--------DTKQPRQYFIGVLDIAGFEI 470
Cdd:cd14907 322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 471 FDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKAT 547
Cdd:cd14907 402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 548 DTSFKNKLYDQHlGKSNNFQKPKPTKGKTeahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA 627
Cdd:cd14907 481 DEKLLNKIKKQH-KNNSKLIFPNKINKDT---FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 628 QaGEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIC 707
Cdd:cd14907 557 D-GSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 708 RKGFPSRILYADFKQRYKVLNasaipegqfidskkasekllgsidvdhTQYKFGHTKVFFK 768
Cdd:cd14907 636 KQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-727 |
1.76e-144 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 462.47 E-value: 1.76e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATIavtGEKKKEEPTS-GKMQGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQA---GDNNLAASVSmGKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 245 SRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMllittnpydyafvsqgeitvp 324
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR--------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 325 siDDQEELMAtdsAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKAAYLTSLNSAD 397
Cdd:cd14900 219 --DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 398 LLKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQL-----DTKQPRQYFIGVLDIAGFEIFD 472
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 473 FNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSF 551
Cdd:cd14900 374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 552 KNKLYdQHLGKSNNFQKPKPTKGKteAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQkssmktlallfSGAQage 631
Cdd:cd14900 453 ASKLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-----------YGLQ--- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 632 ggggkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGF 711
Cdd:cd14900 516 ---------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGF 574
|
650
....*....|....*.
gi 826320982 712 PSRILYADFKQRYKVL 727
Cdd:cd14900 575 PIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-768 |
2.05e-140 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 452.47 E-value: 2.05e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeeptsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA------------GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSN-KKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDS 337
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 338 AVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKAAYLTSLNSADLLKALCYPRVKVGNEFVTKG 417
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 418 QTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 497 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKT 576
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDNESIDFPKVKRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 577 EahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAgEGGGGKKGGKKKGSSFQTVSALFREN 656
Cdd:cd14904 467 Q--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEA-PSETKEGKSGKGTKAPKSLGSQFKTS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 657 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGq 736
Cdd:cd14904 544 LSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK- 622
|
650 660 670
....*....|....*....|....*....|...
gi 826320982 737 fiDSKKASEKLLGSIDVDHT-QYKFGHTKVFFK 768
Cdd:cd14904 623 --DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
24-827 |
1.27e-138 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 453.33 E-value: 1.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 24 RIEAQNKPFDAKTSVFV-------------ADPKESFVKATVQ-SREGGKVTAK---TEGGSTVTVKDDQVF----PMNP 82
Cdd:PTZ00014 16 RRNSNVEAFDKSGNVLKgfyvwtdkapavkEDPDLMFAKCLVLpGSTGEKLTLKqidPPTNSTFEVKPEHAFnansQIDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 83 PKYDkieDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYR-GKKRQEAPPHIFSISDN 161
Cdd:PTZ00014 96 MTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 162 AYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkeeptSGKMQGTLEDQIISANPLLEAFGNAKTVRN 241
Cdd:PTZ00014 173 ALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSK-----------SGNMDLKIQNAIMAANPVLEAFGNAKTIRN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 242 DNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLItTNPYDYAFVSQGEI 321
Cdd:PTZ00014 242 NNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 322 TVPSIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-----PDGTEVADKAAYLTSLNSA 396
Cdd:PTZ00014 321 DVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 397 DLLKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:PTZ00014 401 SLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLY 556
Cdd:PTZ00014 481 EQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 557 DQhLGKSNNFqkpKPTKGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGGGGK 636
Cdd:PTZ00014 561 TN-LKNNPKY---KPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAK 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 637 KggkkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 716
Cdd:PTZ00014 637 G---------QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRT 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 717 YADFKQRYKVLNAsAIPEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFKAGLLGTLEEMRDEKLAQ---LITRTQAI 793
Cdd:PTZ00014 708 FAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEAL 786
|
810 820 830
....*....|....*....|....*....|....
gi 826320982 794 CRGYLMRvefRKMMERRESIFCIQYNIRAFMNVK 827
Cdd:PTZ00014 787 ILKIKKK---RKVRKNIKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-768 |
2.34e-138 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 446.66 E-value: 2.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 178 TGESGAGKTVNTKRVIQYFAtiavtgekkkeEPTSGKMQgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgA 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 258 TGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEML-LITTNPYDYAFVSQGEITVPSI--DDQEELMa 334
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYgLLDPGKYRYLNNGAGCKREVQYwkKKYDEVC- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 335 tdSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEF 413
Cdd:cd14889 228 --NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 414 VTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14889 306 IQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLANEQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 488 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIEL-IEKPMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNF 566
Cdd:cd14889 383 LQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 567 QKpkpTKGKTEAhFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG--AQAGEGGGGKKGGKKKGS 644
Cdd:cd14889 461 GK---SRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTAtrSRTGTLMPRAKLPQAGSD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 645 SF-----QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 719
Cdd:cd14889 537 NFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAE 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 826320982 720 FKQRYKVLnasaIPEGQFIDSKKASEKLLGSIDVdhTQYKFGHTKVFFK 768
Cdd:cd14889 617 FAERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-768 |
1.94e-135 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 437.94 E-value: 1.94e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNAEVvTAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 175 ILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQG------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 249 KFIRIHFGATG-KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLItTNPYDYAFVSQ-GEITVPSI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 327 DDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKAAYLTSLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 403 CYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 561 GKSNNFQKPKPtKGKTEAhFSLVHYAGTVDYNINGWLDKNKDPLNETVvglyqkssmktlallfsgaqageggggkkggk 640
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDF-------------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 641 kkgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 720
Cdd:cd14891 521 ---EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAEL 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 826320982 721 KQRYKVLNASAI------PEGQFIdskkasEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14891 598 VDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-734 |
9.08e-133 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 432.02 E-value: 9.08e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIM---SNKKPELIEMLLITTN----PYDYAFVSQGEI- 321
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggDEEEHEKYEFHDGITGglqlPNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 322 TVPSIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKAAYLTSLNSADL 398
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 399 LKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 555 LYDQHLGKSN-----NFQKPKPTKGKTEAHFSLVHYAGTVDYNI-NGWLDKNKDPLNETVVGLYQkssmktlallfSGAQ 628
Cdd:cd14908 479 LYETYLPEKNqthseNTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFE-----------SGQQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 629 ageggggkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICR 708
Cdd:cd14908 548 ------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVAR 603
|
650 660
....*....|....*....|....*.
gi 826320982 709 KGFPSRILYADFKQRYKVLnASAIPE 734
Cdd:cd14908 604 SGYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-725 |
3.10e-132 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 431.62 E-value: 3.10e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYR--------GKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQGTledQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEmLLITTNPYDYAFVSQGEIT-----VP 324
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSfarkrAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 325 SIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKAAYLTSLNSAD 397
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 398 LLKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLD-------TKQPRQYF--IGVLDIAGF 468
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 469 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKAT 547
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 548 DTSFKNKLYDQHLGksnnfqkpkptkgktEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTL-ALLFSG 626
Cdd:cd14902 472 NQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVvAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 627 AQAGEGGGGKKGGKKKGSSFQT--VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 704
Cdd:cd14902 537 NRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAV 616
|
650 660
....*....|....*....|.
gi 826320982 705 RICRKGFPSRILYADFKQRYK 725
Cdd:cd14902 617 RIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-768 |
5.01e-125 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 410.88 E-value: 5.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNaevVTAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 170 RENQSILITGESGAGKTVNTKRVIQYfatIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNY---LAESSKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 250 FIRIHFG-----ATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPE-LIEMLLITTNPYDYAFVSQGEITV 323
Cdd:cd14895 155 FVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 324 --PSIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA----------------- 384
Cdd:cd14895 235 rnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqh 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 385 -DKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQY----- 458
Cdd:cd14895 315 lDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 459 ------FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPM 531
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 532 GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKptKGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGL 611
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 612 YQKSSMKTLALLFSGAQAGEGGGGKKGGKKKGSSFQTVSAL-----FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAM 686
Cdd:cd14895 551 LGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVgigsqFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 687 EHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegQFIDSKKASEkLLGSIDVDHTQykFGHTKVF 766
Cdd:cd14895 631 DMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGKTRVF 702
|
..
gi 826320982 767 FK 768
Cdd:cd14895 703 LR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-768 |
2.59e-124 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 407.07 E-value: 2.59e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeeptSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAK-----------SGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTnPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEF 413
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 414 VTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 494 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNnfqKPKPT 572
Cdd:cd14876 389 DIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNG---KFKPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 573 KGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG--AQAGEGGGGkkggkkkgssfQTVS 650
Cdd:cd14876 464 KVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGvvVEKGKIAKG-----------SLIG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 651 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAs 730
Cdd:cd14876 533 SQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL- 611
|
650 660 670
....*....|....*....|....*....|....*...
gi 826320982 731 AIPEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14876 612 GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-768 |
6.63e-121 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 397.23 E-value: 6.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIavtgEKKKEEPTSGKMQGTLedqiisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgATG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVL--------PILESFGHAKTILNANASRFGQVLRLHL-QHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLItTNPYDYAFVSQGEI-TVPSIDDQEELMATDSA 338
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVADKAAYLtsLNSADLLKALCYPRVKVGN-EFV 414
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLL--QVPPERLEGAVTHRVTETPyGRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 415 TKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 492
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 493 NHHMFVLEQEEYKKEGIEWEFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPK- 570
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQl 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 571 --PTkgkteahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGGGGKKGgkkkgssfqT 648
Cdd:cd14896 463 plPV-------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP---------T 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 649 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 728
Cdd:cd14896 527 LASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG 606
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 826320982 729 ASAIPEgqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14896 607 SERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-727 |
6.35e-114 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 377.65 E-value: 6.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 178 TGESGAGKTVNTKRVIQYFATIAVTgekkKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS----PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 258 TGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSN-KKPELIEMLLitTNPYDYAFVSQGEITVpsidDQEELMATD 336
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHL--PEGAAFSWLPNPERNL----EEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 337 SAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEf 413
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQ- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 414 vtkgqtvQQVYNAV----------GALAKAIYEKMFLWMVTRINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCIN 482
Cdd:cd14880 312 -------QQVFKKPcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCIN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLG 561
Cdd:cd14880 385 YANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 562 KSNNFQKPKPTKgktEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQagEGGGGKKGGKK 641
Cdd:cd14880 464 GNPCLGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP--EEKTQEEPSGQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 642 KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 721
Cdd:cd14880 539 SRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFV 618
|
....*.
gi 826320982 722 QRYKVL 727
Cdd:cd14880 619 ERYKLL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-730 |
7.25e-110 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 368.15 E-value: 7.25e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFatIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT- 258
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 259 GKLASADIETYLLEKSRVTFQLQAER-SYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITVPSIDDQ-------- 329
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 330 -------EELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKAAYLTSLNSADLL 399
Cdd:cd14906 241 nnktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 400 KALCYPRVKVGNE--FVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRIN----QQLDTKQPRQY-------FIGVLDIA 466
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 467 GFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 545
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 546 ATDTSFKNKlYDQHLGKSNNFQKPKPTKGKteahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFS 625
Cdd:cd14906 480 GSEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 626 gaqagEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIR 705
Cdd:cd14906 555 -----QQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIK 629
|
650 660
....*....|....*....|....*
gi 826320982 706 ICRKGFPSRILYADFKQRYKVLNAS 730
Cdd:cd14906 630 VRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-768 |
1.90e-108 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 361.51 E-value: 1.90e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYFATIAVTGEKKkeeptsgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTD------------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYdYAFVSQGEI-TVPSIDDQEELMATDSA 338
Cdd:cd14886 155 GLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCyDAPGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 339 VDILgFTADEKVAIYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVT 415
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 416 KGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 496 MFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyDQHLgKSNNFQkpkPTKG 574
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFI---PGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 575 kTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGGGGKkggkkkgssfQTVSALFR 654
Cdd:cd14886 467 -SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG----------KFLGSTFQ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 655 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL---NASA 731
Cdd:cd14886 536 LSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSS 615
|
650 660 670
....*....|....*....|....*....|....*..
gi 826320982 732 IPEGQfiDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14886 616 QNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-725 |
2.02e-107 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 360.95 E-value: 2.02e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKE-----EPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTnsesiSPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 245 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNK----KPELIEMLLITTNPYDYAFVSQG 319
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 320 EITV--PSIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------D 385
Cdd:cd14899 242 LCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 386 KAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQL--------------- 450
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 451 DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlAACIELIE-K 529
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 530 PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVV 609
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 610 GLYQKSSMKTLALLFSGAQAGEGGGGKKGGKKKGSSFQ---------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNET 680
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRraksaiaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 826320982 681 KTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-768 |
7.29e-105 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 351.80 E-value: 7.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFAtiavtgeKKKEEPTSGKMQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14875 83 GESGSGKTENAKMLIAYLG-------QLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 255 F-GATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGEITV------PSID 327
Cdd:cd14875 156 FdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 328 DQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQReeqaepDGTEVADKAAYLTSLNSADLLKAL---CY 404
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN------DKAQIADETPFLTACRLLQLDPAKlreCF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 405 pRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLC 480
Cdd:cd14875 310 -LVKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 481 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQH 559
Cdd:cd14875 387 INYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 560 LGKSNNFQKPKPTKGKTeahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSgAQAGEGGGGkkgg 639
Cdd:cd14875 466 ANKSPYFVLPKSTIPNQ---FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLS-TEKGLARRK---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 640 kkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 719
Cdd:cd14875 538 -------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQ 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 826320982 720 F-KQRYKVLNASAIPEGQFIDSKKASEKLLGS----IDVDHTQYKFGHTKVFFK 768
Cdd:cd14875 611 FcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-768 |
2.10e-103 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 348.53 E-value: 2.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 182 GAGKTVNTKRVIQYFATIAVTGEKKKeepTSGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGVL---SVEKLN--------AALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 262 ASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFvsqgeITVPSIDDQE------ELMAT 335
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF-----GIVPLQKPEDkqkaaaAFSKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 336 DSAVDILGFTADEKVAIYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKAAYLTSLNSADLLKALCYPRVKVGNE 412
Cdd:cd01386 227 QAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 413 FVT---------------KGQTVQQvynAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN--- 474
Cdd:cd01386 304 QSTtssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsq 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 475 ---SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSI 536
Cdd:cd01386 381 rgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 537 LEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPTKGKTEA-HFSLVHYAGT--VDYNINGWLDKNK-DPLNETVVGLY 612
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 613 QKSSMKTLALLFSG--AQAgeggggkkggkkkgsSFQtvsalfrenLNKLMTNLRSTHPHFVRCIIPN------ETKTPG 684
Cdd:cd01386 540 QESQKETAAVKRKSpcLQI---------------KFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkdERSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 685 AMEHELVLH------QLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL----NASAIPEGQFIDSKKASEKLLGSIDVD 754
Cdd:cd01386 596 PAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLE 675
|
730
....*....|....
gi 826320982 755 HTQYKFGHTKVFFK 768
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-768 |
2.91e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 314.83 E-value: 2.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 178 TGESGAGKTVNTKRVIQYFATiavtgekkkeepTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 258 TGK-LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITtNPYDYAFVSQGE----ITVPSIDDQEEL 332
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 333 MATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNE 412
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 413 FVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 489 QQFFNHHMFVLEQEEYKKEGIEWEFI-DFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQ 567
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMETAySPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSL-LESSNTNA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 568 KPKPTKG--------KTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFsgaqageggggkkgg 639
Cdd:cd14878 468 VYSPMKDgngnvalkDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF--------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 640 kkkGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 719
Cdd:cd14878 533 ---QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSD 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 826320982 720 FKQRYKVLnASAIPEGQfidsKKASEKLLGSIDVDHTQ---YKFGHTKVFFK 768
Cdd:cd14878 610 FLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-731 |
1.28e-91 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 310.29 E-value: 1.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlPVYNAEVVTAYRgKKRQEAPPHIFSISDNAYQFMLTdRENQSILITGE 180
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFatiaVTGEKKKEeptsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgaTGK 260
Cdd:cd14898 78 SGSGKTENAKLVIKYL----VERTASTT---------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKpeliemLLITTNPYDYAFVSQGEITVpsIDDQEELMATDSAVD 340
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 341 ILGFTADEkvAIYKLTGAVMHYGNMKFKQkqreeqaepDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQTV 420
Cdd:cd14898 215 SLGIANFK--SIEDCLLGILYLGSIQFVN---------DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 421 QqVYNAV-------GALAKAIYEKMFLWMVTRINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14898 284 E-VFNTLkqartirNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 494 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKAT--DTSFKNKLYDQHLGKSNNFQKPKp 571
Cdd:cd14898 361 KKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINTKARDKIK- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 572 tkgkteahfsLVHYAGTVDYNINGWLDKNKdplnetvvglyqkssmktlallfsgaQAGEGGGGKKGGKKKGSSFQTVSA 651
Cdd:cd14898 439 ----------VSHYAGDVEYDLRDFLDKNR--------------------------EKGQLLIFKNLLINDEGSKEDLVK 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 652 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 731
Cdd:cd14898 483 YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-768 |
1.55e-90 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 309.25 E-value: 1.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYnaevVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 182 GAGKTVNTKRVIQYFatiaVTGEKKKEEptsgkMQGTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNE-----ISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 262 ASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAVDI 341
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 342 LGFTaDEKVAIYKLTGAVMHYGNMKFKQ-----KQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEFVTK 416
Cdd:cd14937 225 MNMH-DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 417 GQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 497 FVLEQEEYKKEGIEWEFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYDQHLGKSNNFQKPKPTKGKT 576
Cdd:cd14937 384 YEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 577 EAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGGGGKkggkkkgssfQTVSALFREN 656
Cdd:cd14937 459 NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK----------NLITFKYLKN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 657 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYKVLNASAIPEGQ 736
Cdd:cd14937 529 LNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSS 607
|
650 660 670
....*....|....*....|....*....|..
gi 826320982 737 FIDSKKASEKLLGSIDVDhtQYKFGHTKVFFK 768
Cdd:cd14937 608 LTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-768 |
2.47e-87 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 302.72 E-value: 2.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 172 NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKkeeptsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLA--AVSDRRH------GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 252 RIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITtnpYDYafvsqgeitvPSIDDQEE 331
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAG---EGD----------PESTDLRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 332 LMATDSAVDILGftaDEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---AAYLTSLNS----- 395
Cdd:cd14887 220 ITAAMKTVGIGG---GEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 396 -------ADLLKALCYPRVKVGNEFVTKGQTVQQV------YNAVGALA------KAIYEKMFLWMVTRINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLRLALVSRSVretrsfFDLDGAAAardaacKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 457 QY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 516 FGMDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYDQHLGK----SNNFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 569 PKPTKGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTlALLFSGAQAGeggggkkgGKKKGSSFQT 648
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACSTYT-RLVGSKKNSG--------VRAISSRRST 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 649 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 728
Cdd:cd14887 608 LSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKL 687
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 826320982 729 ASAIPEgqFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14887 688 PMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-767 |
1.83e-86 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 297.54 E-value: 1.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 106 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNAEVVTAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 176 LITGESGAGKTVNTKRVIQYFATIAVTGekKKEEPTSGkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHS--KKGTKLSS--------QISAAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 256 GATGKLASADIETYLLEKSRVTfQLQA-ERSYHIFYQIMSNKKPELIEMLLItTNPYDYAFV--SQGEITV--PSIDDQE 330
Cdd:cd14879 158 NERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPlgPGSDDAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 331 ---ELMAtdsAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLTSLNSADLLKALCYP 405
Cdd:cd14879 236 gfqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 406 RVKVGNEFVTkgqtvqqVY-NAVGA------LAKAIYEKMFLWMVTRINQQL-DTKQPRQYFIGVLDIAGFEIFD---FN 474
Cdd:cd14879 313 TKLVRKELCT-------VFlDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 475 SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSFK 552
Cdd:cd14879 386 SLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQML 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 553 NKLyDQHLGKSNNF-QKPKPTKGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVglyqkssmktlALLFSGAQage 631
Cdd:cd14879 465 EAL-RKRFGNHSSFiAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV-----------NLLRGATQ--- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 632 ggggkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGF 711
Cdd:cd14879 530 ---------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEY 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 712 PSRILYADFKQRYKvlnasaiPEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFF 767
Cdd:cd14879 589 VVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-716 |
2.16e-77 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 272.16 E-value: 2.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 172 NQSILITGESGAGKTVNTKRVIQYFATIavtgekkkeeptSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI------------QTDSQMTeRIDKLIYINNILESMSNATTIKNNNSSRCGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 251 IRIHF---------GATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITTNPYDYAFVSQGE- 320
Cdd:cd14884 149 NLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 321 -----------ITVPSIDDQEELMATDSA-----VDILGFTADEKVAI---YKLTGAVMHYGNMKFKQkqreeqaepdgt 381
Cdd:cd14884 229 hqkrsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 382 evadkAAYLTSLNSADLLKALCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRIN---------QQLDT 452
Cdd:cd14884 297 -----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 453 KQPRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIdfgmDLAACIELIEK 529
Cdd:cd14884 372 EDIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSD----VAPSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 530 PMGIFSILEEECMFP----KATDTSFKNKLYD----QHLGKSNNFQK--PKPTKGKTEAH------FSLVHYAGTVDYNI 593
Cdd:cd14884 448 IAKIFRRLDDITKLKnqgqKKTDDHFFRYLLNnerqQQLEGKVSYGFvlNHDADGTAKKQnikkniFFIRHYAGLVTYRI 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 594 NGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGeggggkkggkkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVR 673
Cdd:cd14884 528 NNWIDKNSDKIETSIETLISCSSNRFLREANNGGNKG--------------NFLSVSKKYIKELDNLFTQLQSTDMYYIR 593
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 826320982 674 CIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 716
Cdd:cd14884 594 CFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-748 |
4.87e-70 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 248.88 E-value: 4.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNAEVVTAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 181 SGAGKTVNTKRVIQYFATIAVTGekkkeePTSGKMQgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgATGK 260
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVAGGG------PETDAFK-----HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 261 LASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKP-ELIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14881 145 LYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYkltGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAAYLTSLNSADLLKALcYPRVKVgnefvTKGQT 419
Cdd:cd14881 225 GILGIPFLDVVRVL---AAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGL-TTRTHN-----ARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 420 VQQVYNA------VGALAKAIYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14881 295 VKSVCDAnmsnmtRDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 489 QQFFNHHMFVLEQEEYKKEGIEWEF-IDFgMDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYDQHlgKSNN- 565
Cdd:cd14881 375 QHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH--RQNPr 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 566 FQKPKPTKGKTeahFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKtlallFsgaqageggggkkggkkkgsS 645
Cdd:cd14881 451 LFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCN-----F--------------------G 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 646 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14881 503 FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYR 582
|
650 660
....*....|....*....|...
gi 826320982 726 VLnASAIPEGQFIDSKKASEKLL 748
Cdd:cd14881 583 LL-APFRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-768 |
3.42e-67 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 240.80 E-value: 3.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 182 GAGKTVNTKRVIQYFATIavtgekkkeeptsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYL-------------GDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 262 ASADIETYLLEKSRVTFQLQAERSYHIFYQIMS--NKKPELIEMLLITTNPYDYAFVSQG-------------EITVPSI 326
Cdd:cd14882 150 SGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 327 DDQEELMAtdsavdILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKAAYLTSLNSADLLKALCYPR 406
Cdd:cd14882 230 KEFEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 407 VKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCI 481
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEecmfpKATDTSFKNKLYDQHLG 561
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 562 KSNNFQKPkptkgKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAgeggggkkggkk 641
Cdd:cd14882 455 KHSQFVKK-----HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 642 kgSSFQTVSALFR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 717
Cdd:cd14882 518 --RNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 826320982 718 ADFKQRYKVLnasAIPEGQFIDSKKASEKLLgSIDVDHTQYKFGHTKVFFK 768
Cdd:cd14882 596 QEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-727 |
1.14e-66 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 239.00 E-value: 1.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 180 ESGAGKTVNTKRVIQYfatiaVTGEKKKEEPTSgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKY-----LTSQPKSKVTTK---------HSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 260 KLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAV 339
Cdd:cd14874 138 LTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 340 DILGFTADEKVAIYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKA-----AYLTSLNSADLLKALCyPRVKVGNEFv 414
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 415 tkgqTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 494 HHMFVLEQEEYKKEGIEwefIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSnNFQK 568
Cdd:cd14874 368 KHSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 569 pkpTKGKTEAHFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAQAGEGGGGKKGGKKKGSSFQT 648
Cdd:cd14874 444 ---ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVSQAQFILRGAQE 520
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 649 VSalfrENLNKlmtnlrsTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 727
Cdd:cd14874 521 IA----DKING-------SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-725 |
4.34e-65 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 237.18 E-value: 4.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 173 QSILITGESGAGKTVNTKRVIQYFATIavtGEKKKEEPTSGKMQGTLE---DQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEI---GDETEPRPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKK--PELIEMLLITTNPYDYAFVSQG--EITVPS 325
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 326 ID--DQEELMATDSAVDIlgfTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKAAYLTSLNSADLLKA 401
Cdd:cd14893 241 LDarDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCALKDPAQILLAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 402 --LCYPRVKVGNEFVT---------------KGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQL----DTKQPRQYFI 460
Cdd:cd14893 318 klLEVEPVVLDNYFRTrqffskdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 461 G-----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE-------FIDFGMDLAACIEL 526
Cdd:cd14893 398 NsqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 527 IE-KPMGIFSILEEECMFPKATDTSFKNKLYDqhlGKSNNFQKPKPTKGKTEAH------------FSLVHYAGTVDYNI 593
Cdd:cd14893 478 FEdKPFGIFDLLTENCKVRLPNDEDFVNKLFS---GNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 594 NGWLDKNKDPLNETVVGLYQKSSMKTL----ALLFSGAQAGEGGGGKKGGKKKGSSFQTVSALFRENLN----------- 658
Cdd:cd14893 555 KGLSSKNMLSISSTCAAIMQSSKNAVLhavgAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvyn 634
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 659 ---KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14893 635 qadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-711 |
1.96e-64 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 233.45 E-value: 1.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 185 KTVNTKRVIQYFATIAVTGEKkkeeptsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASA 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 265 DIETYLLEKSRVTFQLQAERSYHIFYQIMSN-KKPELIEMLLITTNPYDYaFVSQGEITVPSIDDQEELMATDSAVDILG 343
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 344 FTADEKVAIYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKaaylTSLNSadLLKALCYPRVKVGNEFVT-KGQTVQQ 422
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDR----TLIES--LSHNITFDSTKLENILISdRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 423 VYNAVGALAKAIYEKMFLWMVTRINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 501 QEEYKKEGIEWEFIDFGMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLydqhlgksNNFQKPKPTKGKTEAHF 580
Cdd:cd14905 376 QREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKPNKF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 581 SLVHYAGTVDYNINGWLDKNKDP-------------------------LNETVVGLYQ---------KSSMKTLALLFS- 625
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdakntakKSPLSIVKVLLSc 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 626 --------------GAQAGEGGGGKKGGKKKGSSFQTVSAlfrenLNKLMTNlRSTHPHFVRCIIPNETKTPGAMEHELV 691
Cdd:cd14905 525 gsnnpnnvnnpnnnSGGGGGGGNSGGGSGSGGSTYTTYSS-----TNKAINN-SNCDFHFIRCIKPNSKKTHLTFDVKSV 598
|
650 660
....*....|....*....|
gi 826320982 692 LHQLRCNGVLEGIRICRKGF 711
Cdd:cd14905 599 NEQIKSLCLLETTRIQRFGY 618
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-253 |
8.74e-61 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 206.04 E-value: 8.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 122 FCVTVNPYKWLPVYNAEVV-TAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 201 VTGEKKKEEPTS---GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 253
Cdd:cd01363 81 FNGINKGETEGWvylTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-766 |
4.70e-46 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 178.88 E-value: 4.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 179 GESGAGKTVNTKRVIQYFA-----------TIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 248 GKFIRIHFgATGKLASADIETYLLEKSRVTFQLQAERSYHIFYQIMSNKKPELIEMLLITtNPYDYAFVSQGEITVPSID 327
Cdd:cd14938 161 SKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 328 DQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGN-------------MKFKQKQREEQAEPDGTEVADKAAYLTSLN 394
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNINYETILSELENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 395 SADLL---KALCYPRVKVGNEFVT----------KGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYF-- 459
Cdd:cd14938 319 VKNLLlacKLLSFDIETFVKYFTTnyifndsiliKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 460 -IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM--GIFSI 536
Cdd:cd14938 399 yINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 537 LEEECMfPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKTEAhFSLVHYAGTVDYNINGWLDKNKDPLNETVVGLYQKSS 616
Cdd:cd14938 479 LENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 617 ---MKTLALLFSGAQAGEGGGGKKG----------GKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTP 683
Cdd:cd14938 557 neyMRQFCMFYNYDNSGNIVEEKRRysiqsalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKRE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 684 -GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipegqfiDSKKASEKLLGSIDVDHTQYKFGH 762
Cdd:cd14938 637 lCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGN 707
|
....
gi 826320982 763 TKVF 766
Cdd:cd14938 708 NMIF 711
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1591 |
6.30e-27 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 120.17 E-value: 6.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 867 KSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAED--EEEINA------EL 938
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRvkekigEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 939 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEnkvknltEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDK 1018
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL-------AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1019 VNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEd 1098
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1099 eqavgmQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISER---LEEAGGATSAQIEMNKKREAEFQK 1175
Cdd:TIGR02169 452 ------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraSEERVRGGRAVEEVLKASIQGVHG 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1176 MRRDLEEATLQHEA---TAAALRKKHA----DSVAElgEQIDNLQRVK------------QKLEKEKSELKM-------- 1228
Cdd:TIGR02169 526 TVAQLGSVGERYATaieVAAGNRLNNVvvedDAVAK--EAIELLKRRKagratflplnkmRDERRDLSILSEdgvigfav 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1229 ---EIDD--------------LASNMETVSKAKGNF--------------------------EKMCRTLEDQLSEVKTKE 1265
Cdd:TIGR02169 604 dlvEFDPkyepafkyvfgdtlVVEDIEAARRLMGKYrmvtlegelfeksgamtggsraprggILFSRSEPAELQRLRERL 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1266 EEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLL 1345
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1346 REQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIhrtEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQN 1425
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1426 EVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENK 1505
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1506 NLQQEISDLTEQIAEGGKHIHE----------LEKVKKQIDQEKSELQAsLEEAE--ASLEHEEGKILRIQLELNQVKSE 1573
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRA-LEPVNmlAIQEYEEVLKRLDELKEKRAKLE 999
|
810
....*....|....*....
gi 826320982 1574 IDRK-IAEKDEEIDQLKRN 1591
Cdd:TIGR02169 1000 EERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
926-1744 |
1.16e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.39 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 926 ERAEDEEEINAELTAKKRKLedecseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAH 1005
Cdd:TIGR02168 210 EKAERYKELKAELRELELAL------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1006 QQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKK 1085
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1086 EFEMSNLQSKIEDEQAVGMQLQKKIKELqarteeleeeieaeRASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEm 1165
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQL--------------ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1166 nKKREAEFQKMRRDLEEatlqheataaalrkkHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKG 1245
Cdd:TIGR02168 429 -KLEEAELKELQAELEE---------------LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1246 NFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESG-EFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQ---- 1320
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNelgr 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1321 -----LEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAE---------------LQRGMSKANSEVAQWR------ 1374
Cdd:TIGR02168 573 vtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddLDNALELAKKLRPGYRivtldg 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1375 -------------TKYETDAIHRTEELEEAKKKLAQrlqdAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAAC 1441
Cdd:TIGR02168 653 dlvrpggvitggsAKTNSSILERRREIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1442 IALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEG 1521
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1522 -------GKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDrKIAEKDEEIDQLKRNHLR 1594
Cdd:TIGR02168 809 raeltllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1595 VVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLkdtqlhLDDAIRSQDDLKEQLA 1674
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYSLTLEEAEALEN 961
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1675 MVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEME 1744
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1147-1873 |
2.81e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.77 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1147 EISERLEEAGGATSAqiemNKKREAEFQKMRRDLEEATLQHEataaalRKKHADSVAELGEQIDNLQRVKQKLEKEKSEL 1226
Cdd:TIGR02168 217 ELKAELRELELALLV----LRLEELREELEELQEELKEAEEE------LEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1227 KMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRG 1306
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1307 KQAFTQQIEELKRQLEEETKAKNALAHAVQSAR----------HDCDLLREQYEEEQEA---------KAELQRGMSKAN 1367
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNneierlearlERLEDRRERLQQEIEEllkkleeaeLKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1368 SEVAQWRTKYEtDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDL----------------- 1430
Cdd:TIGR02168 447 EELEELQEELE-RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkallknqsglsgilgvl 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1431 -----------------------MIDVERSNAA--CIALDkKQRNFDKV----LAEWKHKY-EETQAELEASQKESRSLS 1480
Cdd:TIGR02168 526 selisvdegyeaaieaalggrlqAVVVENLNAAkkAIAFL-KQNELGRVtflpLDSIKGTEiQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1481 TELFKVKNAYE-------------ETLDQLETLKRENK-------------------------------NLQQEISDLTE 1516
Cdd:TIGR02168 605 KDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1517 QIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRkiaeKDEEIDQLKRNHLRVV 1596
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1597 ESMQSTLDAEIRSRNDALRIKKKMEgdlnEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMV 1676
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1677 ERRANLMQAEVEELRASLEQtersrkmAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEK 1756
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1757 AKKAItdaammaEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLAL-------KGGKKQIQKLEARVRELENEVE 1829
Cdd:TIGR02168 910 RSELR-------RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeeaealeNKIEDDEEEARRRLKRLENKIK 982
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 826320982 1830 GEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKL 1873
Cdd:TIGR02168 983 ELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1108-1911 |
3.22e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 114.78 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1108 KKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatsAQIEMNKKReaEFQKMRRDLEEAtlqh 1187
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKREY---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1188 EATAAALRKKHAD-SVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKakgnfeKMCRTLEDQLSEVKTKee 1266
Cdd:TIGR02169 224 EGYELLKEKEALErQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEK-- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1267 eqqrlINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLR 1346
Cdd:TIGR02169 296 -----IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1347 EQYEEEQEAKAELQRgmskansEVAQWRTKYEtDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNE 1426
Cdd:TIGR02169 371 AELEEVDKEFAETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1427 VEDLMIDVErsnaaciALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTElfkvknayeetLDQLETLKRENKN 1506
Cdd:TIGR02169 443 KEDKALEIK-------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-----------LAEAEAQARASEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1507 LQQEISDLTEQIAEGGKHIHELekvKKQIDQEKSELQASLEEAEAS------LEHEEGKILRIQ------------LELN 1568
Cdd:TIGR02169 505 RVRGGRAVEEVLKASIQGVHGT---VAQLGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLN 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1569 QVKSE--IDRKIAEK------------DEEIDQLKRNHLR---VVESMQS-----------TLDAEI-----------RS 1609
Cdd:TIGR02169 582 KMRDErrDLSILSEDgvigfavdlvefDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1610 RNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEE 1689
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1690 LRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISH-----IQGEMEDIVQE-------ARNAEEKA 1757
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeIQAELSKLEEEvsriearLREIEQKL 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1758 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELENEVEGEQRRNVE 1837
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDE 893
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1838 AVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNvNLARFRKIQHELEEAEER 1911
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEE 966
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-713 |
3.65e-25 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 114.07 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVTFQL------QAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 292 IMS--NKKPEL----IEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATD--------SAVDILGFTADEKVAIYKLTG 357
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 358 AVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLTSLNSADLL-KALCYPRVKVGNEFVTKGQTVQ--QVYNAVGALA 431
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 432 KAIYEKMFLWMVTRINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 495 HMFVLEQEEYKKEGIEWEfidfgmdlAACIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYDQHLGKSNNFQKP 569
Cdd:cd14894 569 VIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 570 KPTKGKTEAH-----------FSLVHYAGTVDYNINGWLDKNKDPL-NETVVGLYQKSSMKTLALLFSGAQAG----EGG 633
Cdd:cd14894 641 EPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGwspnTNR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 634 GGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 713
Cdd:cd14894 721 SMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSSSS 800
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1610 |
4.88e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 110.92 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 845 AETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEA 924
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 925 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLaKEKKALQEA 1004
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL-ELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1005 HQQTLddlqaeEDKVNTLTKAKTKLEQQVDDLEGSLE--QEKKLRMDLERAKRKLEGdlklAQESTMDIENDKQQLDEKL 1082
Cdd:TIGR02168 401 EIERL------EARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELEE----LQEELERLEEALEELREEL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1083 KKKEFEMSNLQSKIEdeqavgmQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISER------LEEAG 1156
Cdd:TIGR02168 471 EEAEQALDAAERELA-------QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyeaaIEAAL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1157 GATSAQIEMNKKREAefqkmrRDLEEATLQHEATAAAL----RKKHADSVAELGEQIDNLQRVKQ---KLEKEKSELKME 1229
Cdd:TIGR02168 544 GGRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGvakDLVKFDPKLRKA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1230 I----------DDLASNMETVSKAKGNFekMCRTLEDQLS------------------EVKTKEEEQQRLINELSAQKAR 1281
Cdd:TIGR02168 618 LsyllggvlvvDDLDNALELAKKLRPGY--RIVTLDGDLVrpggvitggsaktnssilERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1282 LHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQR 1361
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1362 GMSKANSEVAQWRTKYetdaihrtEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAAC 1441
Cdd:TIGR02168 776 ELAEAEAEIEELEAQI--------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1442 IALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEG 1521
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1522 GKHIHELE-KVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDR-------------KIAEKDEEIDQ 1587
Cdd:TIGR02168 928 ELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeyeELKERYDFLTA 1007
|
810 820
....*....|....*....|....*.
gi 826320982 1588 LKRNHLRVVESMQST---LDAEIRSR 1610
Cdd:TIGR02168 1008 QKEDLTEAKETLEEAieeIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1312-1911 |
8.67e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.03 E-value: 8.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1312 QQIEELKRQ-----------LEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVaqwrtkyetd 1380
Cdd:COG1196 200 RQLEPLERQaekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1381 aihrtEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKH 1460
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1461 KYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKS 1540
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1541 ELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRnhlrvvesmqstLDAEIRSRNDALRIKKKM 1620
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL------------LEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1621 EGDLNEMEIQLNHANRQASEAirnlrntQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERS 1700
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAA-------LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1701 RKmaeQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEA-----RNAEEKAKKAITDAAMMAEELKKEQ 1775
Cdd:COG1196 566 LK---AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADaryyvLGDTLLGRTLVAARLEAALRRAVTL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1776 DTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQ 1855
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 1856 TEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLArfrKIQHELEEAEER 1911
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE---ELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1262-1933 |
1.18e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.76 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1262 KTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQlsrgkqafTQQIEELKRQLEEetKAKNALAHAVQSARHD 1341
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEK--------AERYKELKAELRE--LELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1342 CDLLREQYEEEQEAKAELQRGMSKANSEVaqwrtkyetdaihrtEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQ 1421
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKL---------------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1422 RLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLK 1501
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1502 RENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLE--------LNQVKSE 1573
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeelerLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1574 IDRKIAEKDEEIDQLKRNH------LRVVESMQSTLDAEIRSRNDALRIKKKMEGDL----------NEMEIQLNHA--- 1634
Cdd:TIGR02168 466 LREELEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIEAAlgg 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1635 NRQA-----------------------------------------SEAIRNLRNTQGVLKD-----TQLH---------- 1658
Cdd:TIGR02168 546 RLQAvvvenlnaakkaiaflkqnelgrvtflpldsikgteiqgndREILKNIEGFLGVAKDlvkfdPKLRkalsyllggv 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1659 -----LDDAIR-------------------------SQDDLKEQLAMVERRANL--MQAEVEELRASLEQTERSRKMAEQ 1706
Cdd:TIGR02168 626 lvvddLDNALElakklrpgyrivtldgdlvrpggviTGGSAKTNSSILERRREIeeLEEKIEELEEKIAELEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1707 ELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1786
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1787 NMEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRL 1866
Cdd:TIGR02168 786 ELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1867 QDLVDKLQTKVKAYKRQAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1933
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1143-1933 |
4.20e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.85 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1143 RELEEISERLEEAGGATSAQIEMNKKREAE------FQKMRRDLEEAtlqhEATAAALRKKHAD-SVAELGEQIDNLQRV 1215
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREY----EGYELLKEKEALErQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1216 KQKLEKEKSELKMEIDDLASNMETVSKakgnfeKMCRTLEDQLSEVKTKeeeqqrlINELSAQKARLHTESGEFSRQLDE 1295
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEK-------IGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1296 KEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRgmskansEVAQWRT 1375
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1376 KYEtDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVErsnaaciALDKKQRNFDKVL 1455
Cdd:TIGR02169 393 KLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1456 AEWKHKYEETQAELEASQKESRSLSTELfkvknayeetlDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELekvKKQI 1535
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVLKASIQGVHGT---VAQL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1536 DQEKSELQASLEEAEAS------LEHEEGKILRIQ------------LELNQVKSE-IDRKIAEKDEEIDQL-------K 1589
Cdd:TIGR02169 531 GSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILSEDGVIGFAvdlvefdP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1590 RNHLRVVESMQSTLDAEIRSRNDALRIKKKM---EGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQ 1666
Cdd:TIGR02169 611 KYEPAFKYVFGDTLVVEDIEAARRLMGKYRMvtlEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1667 DDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVqllhtqntslintkKKLETDISHIQGEMEdi 1746
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDLSSLEQEIE-- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1747 vqearNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknmeqtvkDLQHRLDEAEQLALKGgKKQIQKLEARVRELEN 1826
Cdd:TIGR02169 755 -----NVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSKL-EEEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1827 EVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQsNVNLARFR-KIQHEL 1905
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR-LGDLKKERdELEAQL 898
|
810 820
....*....|....*....|....*...
gi 826320982 1906 EEAEERADIAESQVNKLRVKSREVHTKI 1933
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1264-1829 |
5.97e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1264 KEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCD 1343
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1344 LLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRL 1423
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1424 QNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRE 1503
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1504 NKNLQQEISDLTEQIAEGGKHIHELEkvkkQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDE 1583
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELL----EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1584 EIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAI 1663
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1664 RSQDDLKEQLAMVERRANLMQAEVeeLRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEM 1743
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALR--RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1744 EDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRE 1823
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
....*.
gi 826320982 1824 LENEVE 1829
Cdd:COG1196 772 LEREIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
919-1805 |
1.39e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 106.31 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 919 AKIKEATERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDENIAK 993
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 994 LAKEKKALQEAHQQTLDDLQAEEDKVNTLTKaktkleqqvddlEGSLEQEKKLRmDLERAKRKLEGDLKLAQESTMDIEN 1073
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE------------EEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1074 DKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1153
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1154 EAGGATSAQIEMNKKREAEFQKMRRDLEEAtlqhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELkmeiddl 1233
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL------- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1234 asnmetvskakgnfekmcRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEA-------LVSQLSRG 1306
Cdd:TIGR02169 472 ------------------YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSV 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1307 KQAFtqqieelkrQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRgMSKANSEVAQWRTKYETDAIHRTE 1386
Cdd:TIGR02169 534 GERY---------ATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLP-LNKMRDERRDLSILSEDGVIGFAV 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1387 ELEEAKKKLAQRLQDAEEHVEAVNskcaSLEkTKQRLQNEVEDLMID---VERSNAACIALDkKQRNFDKVLAEWKHKYE 1463
Cdd:TIGR02169 604 DLVEFDPKYEPAFKYVFGDTLVVE----DIE-AARRLMGKYRMVTLEgelFEKSGAMTGGSR-APRGGILFSRSEPAELQ 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1464 ETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQ 1543
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1544 ASLEEAEASLEHEEGKILRIQLELNQVKSEIDR-KIAEKDEEIDQLKRNHLRVVESMQStLDAEIRSRNDALRI----KK 1618
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKEYlekeIQ 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1619 KMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLddairsqDDLKEQLAMVERRANLMQAEVEELRASLEQTE 1698
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------RDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1699 RSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQgeMEDIVQEARNAEEKAKKAITDAAMMA-EELKKEQDT 1777
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL--SLEDVQAELQRVEEEIRALEPVNMLAiQEYEEVLKR 987
|
890 900
....*....|....*....|....*...
gi 826320982 1778 SAHLERMKKNMEQTVKDLQHRLDEAEQL 1805
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
980-1865 |
1.88e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 105.54 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 980 LTEEMAGLDENIAKLAKEKKALQEAHQQtLDDLQAEEDKVNtltkaktkleQQVDDLEGslEQEKKLR-MDLERAKRKLE 1058
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKR----------QQLERLRR--EREKAERyQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1059 GDLKLAQESTMD-----IENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKEL-QARTEELEEEIEAERASRA 1132
Cdd:TIGR02169 225 GYELLKEKEALErqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1133 KAEKQRSDLSRELEEISERL---EEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI 1209
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1210 DNLQRVKQKLEK---EKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEqqrLINELSAQKARLHTES 1286
Cdd:TIGR02169 385 DELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---KALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1287 GEFSRQLDEKEALVSQLSRgkqaFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLRE-------------QYEEEQ 1353
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDR----VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgtvaqlgSVGERY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1354 EAKAELQRGMSKANSEVAQwrtkyETDAIHRTEELEEAK---------KKLAQRLQDAEE-HVEAVNSKCASLEKTKQRL 1423
Cdd:TIGR02169 538 ATAIEVAAGNRLNNVVVED-----DAVAKEAIELLKRRKagratflplNKMRDERRDLSIlSEDGVIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1424 QNEV----------------EDLMIDVERSNAACIALDK---------KQRNFDKVLAEWKHKYEETQAELEASQKESRS 1478
Cdd:TIGR02169 613 EPAFkyvfgdtlvvedieaaRRLMGKYRMVTLEGELFEKsgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1479 LSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEG 1558
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1559 KILRIQLELNQVKSEIDR-KIAEKDEEIDQLKRNHLRVVESMQSTldaeirsrndalrikkkmEGDLNEMEIQLnhanRQ 1637
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREI------------------EQKLNRLTLEK----EY 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1638 ASEAIRNLRNtqgvlkdtqlhlddairSQDDLKEQLAMVErranlmqAEVEELRASLEQTERSRKMAEQELLDASERvql 1717
Cdd:TIGR02169 831 LEKEIQELQE-----------------QRIDLKEQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLESR--- 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1718 lhtqntslintKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQtvkdlqh 1797
Cdd:TIGR02169 884 -----------LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE------- 945
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1798 rlDEAEQLALKGGKKQIQKLEARVRELE-------NEVEGEQRRNVEAVKSLRKHERR---VKELTYQTEEDRKNVLR 1865
Cdd:TIGR02169 946 --IPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEErkaILERIEEYEKKKREVFM 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
865-1431 |
7.45e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRK 944
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 945 LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTK 1024
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1025 AKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGM 1104
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1105 QLQKKIKELQARTEELEEEIEAERASRAKAEKQR---------SDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQK 1175
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1176 mRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELkmEIDDLASNMETVSKAKGNFEKMCRTLE 1255
Cdd:COG1196 568 -AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV--LGDTLLGRTLVAARLEAALRRAVTLAG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1256 DQLSEVKTKEEEQQRLINELSAQKARLhtesgefsRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAV 1335
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELL--------AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1336 QSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAqwrtKYETDAIHRTEELEEAKKKLAQRLQD-------AEEHVEA 1408
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEE 792
|
570 580
....*....|....*....|...
gi 826320982 1409 VNSKCASLEKTKQRLQNEVEDLM 1431
Cdd:COG1196 793 LEERYDFLSEQREDLEEARETLE 815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
867-1598 |
1.87e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.45 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 867 KSEAKRKELEEKMVTLMQE----KNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAEltAKK 942
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKaeeaKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE--EKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 943 RKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDENIAKLAKEKKALQEAhqqtlddlqaeedkvntl 1022
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAK---KKAEEAKKADEAKKK--AEEAKKKADAAKKKAEEAKKAAEA------------------ 1347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1023 tkAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAV 1102
Cdd:PTZ00121 1348 --AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1103 GMQLQKKIKELQARTEEleeeieaerASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEfqKMRRDLEE 1182
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEE---------AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEE 1494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1183 ATLQ-HEATAAALRKKHADSVAELGEQidnlqrvKQKLEKEKSELKMEIDDlASNMETVSKAkgnfEKMCRTLEDQLSEV 1261
Cdd:PTZ00121 1495 AKKKaDEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADE-AKKAEEKKKA----DELKKAEELKKAEE 1562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1262 KTKEEEQQRlinelSAQKARLHTESGEFSRQLDEKEaLVSQLSRGKQAFTQQIEELKRqlEEETKAKNALAHAVQSARHD 1341
Cdd:PTZ00121 1563 KKKAEEAKK-----AEEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKK 1634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1342 CDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiHRTEEL---EEAKKKLAQRLQDAEEH---VEAVNSKCAS 1415
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaEEDEKKAAEALKKEAEEakkAEELKKKEAE 1713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1416 LEKTKQRLQNEVEDLMIDVERSnaacialdKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAY-EETL 1494
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEEL 1785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1495 DQLETLKR-ENKNLQQEISDLTEQIAEGGKHIHE-LEKVKKQIDQEKSELQAS----LEEAEASLEHEEGKilriqlelN 1568
Cdd:PTZ00121 1786 DEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLvINDSKEMEDSAIKEVADSknmqLEEADAFEKHKFNK--------N 1857
|
730 740 750
....*....|....*....|....*....|
gi 826320982 1569 QVKSEIDRKIAEKDEEIDQLKRNHLRVVES 1598
Cdd:PTZ00121 1858 NENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1169-1913 |
2.99e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1169 REAEFQKMRRDLEEATLQHEATAAALRKKHADSVAElgeqidnlQRVKQKLEKEKSELKMEIDDlASNMETVSKAkgnfE 1248
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAE--------EARKAEEAKKKAEDARKAEE-ARKAEDARKA----E 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1249 KMCRTLEDQLSEVKTKEEEQQRLINELSAQKARlhteSGEFSRQLDEkealVSQLSRGKQAFTQQIEELKRQLEEETKAK 1328
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAK----KAEAARKAEE----VRKAEELRKAEDARKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1329 NALAHAVQSARHDCDLLREQYEEEQEAK-AELQRGmskaNSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAEEHVE 1407
Cdd:PTZ00121 1216 EARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1408 AVNSKCASLEKTKQRLQNEVEDLMIDVErsnaaciaLDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELfkvk 1487
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA---- 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1488 NAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKilriqlel 1567
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-------- 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1568 nqvKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRN 1647
Cdd:PTZ00121 1432 ---KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1648 TQgvlKDTQLHLDDAIRSQDDLKEqlAMVERRAN-LMQAEVEELRASLEQTERSRKMAEQELLDASERVQllHTQNTSLI 1726
Cdd:PTZ00121 1509 KK---KADEAKKAEEAKKADEAKK--AEEAKKADeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1727 NTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQH-RLDEAEQL 1805
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1806 ALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAE 1885
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
730 740 750
....*....|....*....|....*....|.
gi 826320982 1886 EAE---EQSNVNLARFRKIQHELEEAEERAD 1913
Cdd:PTZ00121 1741 EDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
843-1430 |
7.84e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 97.05 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 843 KSAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEA-------DSLADAEERCDQLIKTKI 915
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneierleARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 916 QL-----EAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV---KNLTEEMAGL 987
Cdd:TIGR02168 425 ELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 988 DENIAKLAKEKK-------------------------ALQEAHQQTL-DDLQAEEDKVNTLTKAKTKleqQVDDLEGSLE 1041
Cdd:TIGR02168 505 SEGVKALLKNQSglsgilgvlselisvdegyeaaieaALGGRLQAVVvENLNAAKKAIAFLKQNELG---RVTFLPLDSI 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1042 QEKKLRMDLERAKRKLEGDLKLAQE----------------STMDIENDKQQLDEKLKKKEFEMSN------------LQ 1093
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDlvkfdpklrkalsyllGGVLVVDDLDNALELAKKLRPGYRIvtldgdlvrpggVI 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1094 SKIEDEQAVGMQ-LQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAE 1172
Cdd:TIGR02168 662 TGGSAKTNSSILeRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQ 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1173 FQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCR 1252
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1253 TLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALA 1332
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1333 HAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSK 1412
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD 966
|
650
....*....|....*...
gi 826320982 1413 CASLEKTKQRLQNEVEDL 1430
Cdd:TIGR02168 967 EEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
837-1599 |
1.07e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 96.66 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 837 KIKPLLKSAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMvtlmqekNDLQLQVQAEADSLADAEERCDQLIKTKIQ 916
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-------EELEEQLETLRSKVAQLELQIASLNNEIER 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 917 LEAKIKEATERAEDEEEINAELtaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAK 996
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 997 E---KKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAkrkLEGDLklaQESTMDIEN 1073
Cdd:TIGR02168 483 ElaqLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRL---QAVVVENLN 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1074 DKQQLDEKLKKKEFEMSNLqskIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSD-LSRELeeISERL 1152
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTF---LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYlLGGVL--VVDDL 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1153 EEAggatsaqIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHadSVAELGEQIDNLQRVKQKLEKEKSELKMEIDD 1232
Cdd:TIGR02168 632 DNA-------LELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNS--SILERRREIEELEEKIEELEEKIAELEKALAE 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1233 LasnmetvskakgnfEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQ 1312
Cdd:TIGR02168 703 L--------------RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1313 QIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYEtDAIHRTEELEEAK 1392
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA-ATERRLEDLEEQI 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1393 KKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEAS 1472
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1473 QKESRSLSTELF----KVKNAYEETLDQLETLKR----ENKNLQQEISDLTEQIAEGGK----HIHELEKVKKQIDqEKS 1540
Cdd:TIGR02168 928 ELRLEGLEVRIDnlqeRLSEEYSLTLEEAEALENkiedDEEEARRRLKRLENKIKELGPvnlaAIEEYEELKERYD-FLT 1006
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1541 ELQASLEEAEASLEheegkilriqlelnQVKSEIDRKIAEK-DEEIDQLKRNHLRVVESM 1599
Cdd:TIGR02168 1007 AQKEDLTEAKETLE--------------EAIEEIDREARERfKDTFDQVNENFQRVFPKL 1052
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1003-1925 |
1.33e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 96.34 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1003 EAHQQTLDDLQAEEDKVNTL-TKAKTKLEQQVDDLEGSLEQ---EKKLRMDLERAKRKLEGDLKLAQESTM--------- 1069
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRNQLQNTVheleaakcl 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1070 --DIENDKQQLDEKLKK----KEFEMSNLQSKIED-EQAVGmqlqKKIKELQARTEELEeeieaeRASRAKAEKQRSDLS 1142
Cdd:pfam15921 161 keDMLEDSNTQIEQLRKmmlsHEGVLQEIRSILVDfEEASG----KKIYEHDSMSTMHF------RSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1143 RELEEISERLEEAGGATSA-QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEK 1221
Cdd:pfam15921 231 TEISYLKGRIFPVEDQLEAlKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1222 EKSELKMEIDDLASnmeTVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLdekEALVS 1301
Cdd:pfam15921 311 QNSMYMRQLSDLES---TVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL---QKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1302 QLSRGKQAFTQQIEELKRQLEEETKAKNALAHavqsarhdcdllreqyeeeqeakaeLQRGMSKANSEVAQWRTKYETda 1381
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRLWDRDTGNSITIDH-------------------------LRRELDDRNMEVQRLEALLKA-- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1382 iHRTEELEEAKKKLAQrLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLmidversNAACIALDKKQRNFDKVLAEWKHK 1461
Cdd:pfam15921 438 -MKSECQGQMERQMAA-IQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLTASLQEK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1462 ---YEETQAELEASQKESRSLSTELFKVKNAyEETLDQLET------LKRENKN-----LQQEISDLTEQIAEGGKHIHE 1527
Cdd:pfam15921 509 eraIEATNAEITKLRSRVDLKLQELQHLKNE-GDHLRNVQTecealkLQMAEKDkvieiLRQQIENMTQLVGQHGRTAGA 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1528 LEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQ-----LELNQVK-----SEIDRKIAEKDEEIDQLkRNHLRVVE 1597
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEarvsdLELEKVKlvnagSERLRAVKDIKQERDQL-LNEVKTSR 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1598 SMQSTL--DAEIRSRNdalrIKKKMEgdlnEMEIQLNHANRQASEAIRNLRNTQGVLKdtqlhlddAIRSQDDLKEQLAM 1675
Cdd:pfam15921 667 NELNSLseDYEVLKRN----FRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLK--------SMEGSDGHAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1676 VerranlMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEE 1755
Cdd:pfam15921 731 G------MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1756 KakkaitdAAMMAEELKKEQDTSAHLERMKKNMEQ-TVK-DLQHRLDEAEqlaLKG-GKKQIQKLEARVreLENEVEGEQ 1832
Cdd:pfam15921 805 K-------VANMEVALDKASLQFAECQDIIQRQEQeSVRlKLQHTLDVKE---LQGpGYTSNSSMKPRL--LQPASFTRT 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1833 RRNVEAVKS----LRKHERRVKELTYQTEEDRKNVlrLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLARFRkIQHELEEA 1908
Cdd:pfam15921 873 HSNVPSSQStasfLSHHSRKTNALKEDPTRDLKQL--LQELRSVINEEPTVQLSKAEDKGRAPSLGALDDR-VRDCIIES 949
|
970
....*....|....*..
gi 826320982 1909 EERADIAESQVNKLRVK 1925
Cdd:pfam15921 950 SLRSDICHSSSNSLQTE 966
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1072-1802 |
2.86e-19 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 94.70 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1072 ENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISER 1151
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1152 LEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSELKMEID 1231
Cdd:TIGR04523 112 IK-------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1232 DLASNMETVSKAKgnfekmcRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKqaft 1311
Cdd:TIGR04523 184 NIQKNIDKIKNKL-------LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ---- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1312 QQIEELKrqlEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELqrgmSKANSEVAQ-WRTKYETDAIHRTEELEE 1390
Cdd:TIGR04523 253 TQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNNQKEQdWNKELKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1391 AKKKLAQrlqdAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELE 1470
Cdd:TIGR04523 326 IQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1471 ASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAE 1550
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1551 ASLEHEEGKILRIQ---LELNQVKSEIDRKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIRSRNDALrIKKKMEGDLNEM 1627
Cdd:TIGR04523 482 QNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELKKENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1628 EIQLNHANRQASEairnLRNTQGVLKDTQLHLDDAIR----SQDDLKEQLAM-------VERRANLMQAEVEELRASLEQ 1696
Cdd:TIGR04523 560 EKEIDEKNKEIEE----LKQTQKSLKKKQEEKQELIDqkekEKKDLIKEIEEkekkissLEKELEKAKKENEKLSSIIKN 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1697 TERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKA---KKAITDAAMMAEELKK 1773
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYitrMIRIKDLPKLEEKYKE 715
|
730 740
....*....|....*....|....*....
gi 826320982 1774 EQDTSAHLERMKKNMEQTVKDLQHRLDEA 1802
Cdd:TIGR04523 716 IEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1430 |
4.77e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 838 IKPLLKSAETEKEMANMKEEFEKAKEELAKseAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDqliktkiQL 917
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELE-------EL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 918 EAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKE 997
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 998 KKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQ 1077
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1078 LDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAeKQRSDLSRELEEISERLEEAGG 1157
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1158 ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNm 1237
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA- 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1238 etvSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTEsGEFSRQLDEKEALVSQ-----LSRGKQAFTQ 1312
Cdd:COG1196 591 ---ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLegeggSAGGSLTGGS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1313 QIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAK 1392
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
570 580 590
....*....|....*....|....*....|....*...
gi 826320982 1393 KKLAQRLQDAEEHVEAvnskcASLEKTKQRLQNEVEDL 1430
Cdd:COG1196 747 LLEEEALEELPEPPDL-----EELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1513 |
6.57e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 832 MKLYFKIKPLLKSAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAeercdqlI 911
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA-------A 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 912 KTKIQLEAKIKEATERAEDEEEINAELTAKKRKL-EDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDEN 990
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 991 IAKLAKEKKALQEAHQqtlddlQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGD-LKLAQESTM 1069
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1070 DIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQarteeLEEEIEAERASRAKAEKQRSDLSRELEEIS 1149
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK-----KAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1150 ERLEEaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSElkme 1229
Cdd:PTZ00121 1559 KAEEK------KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---- 1628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1230 iddlasnmETVSKAKGNFEKMCRTLEDQLSEVKtKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQA 1309
Cdd:PTZ00121 1629 --------EEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1310 FTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQyEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEEL- 1388
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKe 1778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1389 ----EEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRlQNEVEDLMIDVERSNAACIAlDKKQRNFDKVLAEWKHKYEE 1464
Cdd:PTZ00121 1779 avieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE-GNLVINDSKEMEDSAIKEVA-DSKNMQLEEADAFEKHKFNK 1856
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 826320982 1465 TQAELEASQKESRSlSTELFKVKNAYEETLDQLETLKRENKNLQQEISD 1513
Cdd:PTZ00121 1857 NNENGEDGNKEADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
894-1536 |
2.01e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.05 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 894 QAEADSLADAEERCDQLIKTKIQLEaKIKEATERAEdeeEINAELTAKKRKLEDECSElKKDIDDLeltLAKVEKEKHAT 973
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQILGLD-DYENAYKNLG---EVIKEIKRRIERLEKFIKR-TENIEEL---IKEKEKELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 974 ENKVKNLTEEMAGLDENIAKLAKEKKALqEAHQQTLDDLQAEEDKVNtltKAKTKLEQQVDDLEGSLEQEKKLRMDLERA 1053
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLE---GSKRKLEEKIRELEERIEELKKEIEELEEK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1054 KRKLEgDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDeqavgmqLQKKIKELqarteeleeeieaerasrak 1133
Cdd:PRK03918 282 VKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-------IEERIKEL-------------------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1134 aekqrSDLSRELEEISERLEEAggatsaqiemnKKREAEFQKMRRDLEEAtLQHEATAAALRKKHAD-SVAELGEQIDNL 1212
Cdd:PRK03918 334 -----EEKEERLEELKKKLKEL-----------EKRLEELEERHELYEEA-KAKKEELERLKKRLTGlTPEKLEKELEEL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1213 QRVKQKLEKE-------KSELKMEIDDLASNMETVSKAKGNFEKMCRTLEdqlsevktkEEEQQRLINELSAQKARLHTE 1285
Cdd:PRK03918 397 EKAKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKCPVCGRELT---------EEHRKELLEEYTAELKRIEKE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1286 SGEFSRQLD----EKEALVSQLSRGKQAFTQ-QIEELKRQLEEETKAKNalahaVQSARHDCDLLREQYEEEQEAKAELq 1360
Cdd:PRK03918 468 LKEIEEKERklrkELRELEKVLKKESELIKLkELAEQLKELEEKLKKYN-----LEELEKKAEEYEKLKEKLIKLKGEI- 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1361 RGMSKANSEVAQWRTKYETdAIHRTEELEEAKKKLAQRLQD-AEEHVEAVNSKCASLEKTKQR---LQNEVEDLMIDVER 1436
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKE 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1437 SNAACIALDKKQRNFDKVLAEWKHKYEE-TQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLT 1515
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
650 660
....*....|....*....|.
gi 826320982 1516 EQIAEGGKHIHELEKVKKQID 1536
Cdd:PRK03918 701 EELEEREKAKKELEKLEKALE 721
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
941-1648 |
6.83e-18 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 90.46 E-value: 6.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 941 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVN 1020
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1021 TLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQ 1100
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1101 AVGMQLQKKIKELQARteeleeeieaerasrakaekqrsdlsreleeiserleeaggatsaqIEMNKKREAEFQkmrrDL 1180
Cdd:TIGR04523 194 NKLLKLELLLSNLKKK----------------------------------------------IQKNKSLESQIS----EL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1181 EEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSkakgnfekmcrTLEDQLSE 1260
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK-----------ELEKQLNQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1261 VKT-----KEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLsrgkqafTQQIEELKRQLEEETKAKNALahav 1335
Cdd:TIGR04523 293 LKSeisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTNSESENSEK---- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1336 qsarhdcdllREQYEEEQEAKAELQRGMSKANSEVaqwrtkyetdaihrtEELEEAKKKLAQRLQDAEEHVEAVNSKCAS 1415
Cdd:TIGR04523 362 ----------QRELEEKQNEIEKLKKENQSYKQEI---------------KNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1416 LEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLD 1495
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1496 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHE--EGKILRIQLELNQVKSE 1573
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQT 576
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1574 ID---RKIAEKDEEIDQLKRNHLRVVeSMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNT 1648
Cdd:TIGR04523 577 QKslkKKQEEKQELIDQKEKEKKDLI-KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
884-1637 |
8.42e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 8.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 884 QEKNDLQLQVQAEADSLAdaeERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKK-RKLEdecsELKKDIDDLELT 962
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKA---EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDaRKAE----EARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 963 LAKVEKEKHATEnkvknlteemagldenIAKLAKEKKALQEAHQQTlddlqaEEDKVNTLTKAktkleQQVDDLEGSLEQ 1042
Cdd:PTZ00121 1156 IARKAEDARKAE----------------EARKAEDAKKAEAARKAE------EVRKAEELRKA-----EDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1043 EKKLRMDlerAKRKLEgDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEE 1122
Cdd:PTZ00121 1209 EEERKAE---EARKAE-DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1123 EIEAERASRakaEKQRSDLSRELEEISERLEEAGGATSAqiemnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSV 1202
Cdd:PTZ00121 1285 KAEEKKKAD---EAKKAEEKKKADEAKKKAEEAKKADEA------KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1203 AElgeQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKgNFEKMCRTLEDQLSEVKTKEEEQQRLinELSAQKARL 1282
Cdd:PTZ00121 1356 AD---EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKA--DEAKKKAEE 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1283 HTESGEFSRQLDEK-----------EALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAvQSARHDCDLLREQYEE 1351
Cdd:PTZ00121 1430 KKKADEAKKKAEEAkkadeakkkaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA-EEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1352 EQEA----KAELQRGMSKANS--------EVAQWRTKYETDAIHRTEELEEAK-KKLAQRLQDAEEHVEAVNSKCASLEK 1418
Cdd:PTZ00121 1509 KKKAdeakKAEEAKKADEAKKaeeakkadEAKKAEEKKKADELKKAEELKKAEeKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1419 TKQRLQNEVEDLMIDVERSNAAcialDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLE 1498
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1499 TLKR---ENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKilRIQLELNQVKSEID 1575
Cdd:PTZ00121 1665 EEAKkaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN--KIKAEEAKKEAEED 1742
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1576 RKIAE---KDEE----IDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQ 1637
Cdd:PTZ00121 1743 KKKAEeakKDEEekkkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1085-1841 |
1.46e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1085 KEFEMSNLQSKIEDEQAvgMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE 1164
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1165 MNKKREAEFQKMR--RDLEEATLQHEA-TAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSElKMEIDDLASNMETVS 1241
Cdd:PTZ00121 1155 EIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1242 KAKGNFEKMCRTLEDQLSEVKTKEEEQQrlINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQL 1321
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1322 EEETKAKNALAHAvQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELE--EAKKKLAQRL 1399
Cdd:PTZ00121 1312 EEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkaDAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1400 QDAEEHVEAV--NSKCASLEKTKQRLQNEVEDLMIDVERSNAACIAldKKQRNFDKVLAEWKHKYEETQAELEASQKESR 1477
Cdd:PTZ00121 1391 KKADEAKKKAeeDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1478 SLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQiAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEE 1557
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1558 GKILRIQLELNqvKSEIDRKIAEKDEEiDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDlnemEIQLNHANRQ 1637
Cdd:PTZ00121 1548 ADELKKAEELK--KAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1638 ASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDL-KEQLAMVERRANLMQAEVEELRASLE---QTERSRKMAEQELLDASE 1713
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEEDKKKAEEakkAEEDEKKAAEALKKEAEE 1700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1714 rvqllhtqntslintKKKLEtdishiqgEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVK 1793
Cdd:PTZ00121 1701 ---------------AKKAE--------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 826320982 1794 DLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKS 1841
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1416-1928 |
1.77e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1416 LEKTKQRLqNEVEDLMIDVER--------SNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVK 1487
Cdd:COG1196 181 LEATEENL-ERLEDILGELERqleplerqAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1488 NAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLEL 1567
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1568 NQVKSEIDR---KIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRN 1644
Cdd:COG1196 340 EELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1645 LRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRanlmQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTS 1724
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAEL----EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1725 LINTKKK--------LETDISHIQGEMEDIVQEARNAEEKAKKAI----------------TDAAMMAEELKKEQD---T 1777
Cdd:COG1196 496 LLEAEADyegflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaalqnivveddEVAAAAIEYLKAAKAgraT 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1778 SAHLERMKKNmEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTE 1857
Cdd:COG1196 576 FLPLDKIRAR-AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1858 EDRKNVLRLQDLVDKLQTKVKAykRQAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSRE 1928
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLE--AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
965-1865 |
1.86e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 89.26 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 965 KVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAhqqtlDDLQAEEDKVNTLTKAKTKL-EQQVDDLEGSLEQE 1043
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEET-----ENLAELIIDLEELKLQELKLkEQAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1044 KKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKkefEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEE 1123
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ---EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1124 IEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVA 1203
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1204 ELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLH 1283
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1284 TESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGM 1363
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1364 SKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKcASLEKTKQRLQNEVEDLMIDVERSNAACIA 1443
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK-LRLLIPKLKLPLKSIAVLEIDPILNLAQLD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1444 LDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNA-----YEETLDQLETLKRENKNLQQEISDLTEQI 1518
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaeKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1519 AEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRN-HLRVVE 1597
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKeEEKSEL 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1598 SMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEairnlrntqgvlKDTQLHLDDAIRSQDDLKEQLAMVE 1677
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE------------EAELLEEEQLLIEQEEKIKEEELEE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1678 RRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETdishIQGEMEDIVQEARNAEEKA 1757
Cdd:pfam02463 838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK----EKEEKKELEEESQKLNLLE 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1758 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVEGEQRRNVE 1837
Cdd:pfam02463 914 EKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKD 993
|
890 900
....*....|....*....|....*...
gi 826320982 1838 AVKSLRKHERRVKELTYQTEEDRKNVLR 1865
Cdd:pfam02463 994 ELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1131-1750 |
3.51e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1131 RAKAEKQRSDLSRELEEISERLEEAGgatsAQIEmNKKREAE----FQKMRRDLEEatLQHEATAAALRKKHADsVAELG 1206
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELE----RQLE-PLERQAEkaerYRELKEELKE--LEAELLLLKLRELEAE-LEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1207 EQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSK-----------AKGNFEKMCRTLEDQLSEVKTKEEEQQRL---I 1272
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELeleeaqaeeyeLLAELARLEQDIARLEERRRELEERLEELeeeL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1273 NELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEE 1352
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1353 QEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKcASLEKTKQRLQNEVEDLMI 1432
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL-AELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1433 DVERSNAACIALDKKQRNFDKVLAEWKHkyeetqAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEiS 1512
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKA------ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDD-E 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1513 DLTEQIA------EGGKHIHELEKVKKQIDQEKSELQASLEEA----EASLEHEEGKILRIQLEL-----NQVKSEIDRK 1577
Cdd:COG1196 558 VAAAAIEylkaakAGRATFLPLDKIRARAALAAALARGAIGAAvdlvASDLREADARYYVLGDTLlgrtlVAARLEAALR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1578 IAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQgvlKDTQL 1657
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL---AEAEE 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1658 HLDDAIRSQDDLKEQLAMVERRANLMQAE------------------VEELRASLEQTERSRK-------MAEQELLDAS 1712
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEeeelleeealeelpeppdLEELERELERLEREIEalgpvnlLAIEEYEELE 794
|
650 660 670
....*....|....*....|....*....|....*...
gi 826320982 1713 ERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEA 1750
Cdd:COG1196 795 ERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLET 832
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1026-1644 |
9.70e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.89 E-value: 9.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1026 KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE--GDLKLAQESTMDIENDKQQLDEklkkkefemsnLQSKIEDEQAvg 1103
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEY-----------LRAALRLWFA-- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1104 mqlQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE-----MNKKRE------AE 1172
Cdd:COG4913 287 ---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1173 FQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQ-------RVKQKLEKEKSELKMEIDDLASNMETVSKakg 1245
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaeaeAALRDLRRELRELEAEIASLERRKSNIPA--- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1246 NFEKMCRTLEDQLS-------------EVKTKEEEQQRLINELsaqkarLHTesgeFSRQL-----DEKEAL--VSQLSR 1305
Cdd:COG4913 441 RLLALRDALAEALGldeaelpfvgeliEVRPEEERWRGAIERV------LGG----FALTLlvppeHYAAALrwVNRLHL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1306 GKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDC-DLLREQYEEEQ-----EAKAELQR--------GMSKANSEVA 1371
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRhpraitraGQVKGNGTRH 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1372 Q------WRTKYET--DAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQN--EVEDLMIDVErsnaac 1441
Cdd:COG4913 591 EkddrrrIRSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVA------ 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1442 iALDKKqrnfdkvLAEWkhkyEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAeg 1521
Cdd:COG4913 665 -SAERE-------IAEL----EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD-- 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1522 gkhihELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQS 1601
Cdd:COG4913 731 -----ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA 805
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1602 TLDAEIRSRNDALRIKKKMEGD------------LNEMEIQ----LNHANRQASEAIRN 1644
Cdd:COG4913 806 DLDADLESLPEYLALLDRLEEDglpeyeerfkelLNENSIEfvadLLSKLRRAIREIKE 864
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
867-1586 |
1.37e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 86.23 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 867 KSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLE 946
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 947 DECSELKKDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKV 1019
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1020 NTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKlegdlklaqesTMDIENDKQQLDEKLKKKEFEMSNLQSKIED- 1098
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ-----------NNQLKDNIEKKQQEINEKTTEISNTQTQLNQl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1099 ---EQAVGMQLQKKIKELQarteeleeeieaerasraKAEKQRSDLSRELEEISERLEEAGgaTSAQIEMNKKREAEFQK 1175
Cdd:TIGR04523 259 kdeQNKIKKQLSEKQKELE------------------QNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1176 MRRDLEEATLQheataaalRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLE 1255
Cdd:TIGR04523 319 QEKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1256 DQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSrgkqaftQQIEELKRQLEEETKAKNALAHAV 1335
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN-------SEIKDLTNQDSVKELIIKNLDNTR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1336 QSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVaqwrtkyetdaihrtEELEEAKKKLAQRLQDAEEHVEAVNSKCAS 1415
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL---------------KKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1416 LEKTKQRLQNEVEDLMIDVER--SNAACIALDKKQRNFDKVLAEWKHkyeeTQAELEASQKESrslstelfkvknayEET 1493
Cdd:TIGR04523 529 LESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQ----TQKSLKKKQEEK--------------QEL 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1494 LDQLETlkrENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHeegkilrIQLELNQVK-- 1571
Cdd:TIGR04523 591 IDQKEK---EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ-------IKETIKEIRnk 660
|
730
....*....|....*.
gi 826320982 1572 -SEIDRKIAEKDEEID 1586
Cdd:TIGR04523 661 wPEIIKKIKESKTKID 676
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
865-1427 |
1.83e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.86 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMvtlmqekndlqlqvqaeadsladaeERCDqliKTKIQLEAKIKEATERAEDEEEINAELTakkrk 944
Cdd:PRK02224 208 LNGLESELAELDEEI-------------------------ERYE---EQREQARETRDEADEVLEEHEERREELE----- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 945 ledecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEkKALQEAHQQTLDDLQAEedkvntltk 1024
Cdd:PRK02224 255 ------TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARREE--------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1025 aktkLEQQVDDLEGSLEQEkklRMDLERAKRKLEGdlklAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGM 1104
Cdd:PRK02224 319 ----LEDRDEELRDRLEEC---RVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1105 QLQKKIKELQARTeeleeeieaerasrAKAEKQRSDLSRELEEISERLEEAggatsaqiemnKKREAEFQKMRRDLEEAT 1184
Cdd:PRK02224 388 ELEEEIEELRERF--------------GDAPVDLGNAEDFLEELREERDEL-----------REREAELEATLRTARERV 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1185 LQHEATAAALR----------KKHADSVAELGEQIDnlqrvkqKLEKEKSELKMEIDDLASNMETVSKAKgNFEKMCRTL 1254
Cdd:PRK02224 443 EEAEALLEAGKcpecgqpvegSPHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1255 EDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAH- 1333
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERi 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1334 -----AVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIhrteelEEAKkklaQRLQDAEEHVEA 1408
Cdd:PRK02224 595 rtllaAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI------EEAR----EDKERAEEYLEQ 664
|
570
....*....|....*....
gi 826320982 1409 VNSKCASLEKTKQRLQNEV 1427
Cdd:PRK02224 665 VEEKLDELREERDDLQAEI 683
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
842-1727 |
2.42e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 82.53 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 842 LKSAETEKEmanmkeefekakeelakseakRKELEEKMvtlmqekNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKI 921
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 922 KEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKAL 1001
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1002 QEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLegDLKLAQEstmdiendkqqldek 1081
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEE--------------- 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1082 lkkkefemSNLQSKIEDEQavgmqlqkkikelqarteeleeeieaeraSRAKAEkqrsdlSREleeiserleeaggatsa 1161
Cdd:pfam01576 614 --------KAISARYAEER-----------------------------DRAEAE------ARE----------------- 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1162 qiemnkkREAEFQKMRRDLEEAtlqheataaalrkkhadsvaelgeqidnlQRVKQKLEKEKSELKMEIDDLASNMETVS 1241
Cdd:pfam01576 634 -------KETRALSLARALEEA-----------------------------LEAKEELERTNKQLRAEMEDLVSSKDDVG 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1242 KAKGNFEKMCRTLEDQLSEVKTKEEEqqrLINELSA-QKARLHTESgefsrqldEKEALVSQLSRGKQAFTQQIEELKRQ 1320
Cdd:pfam01576 678 KNVHELERSKRALEQQVEEMKTQLEE---LEDELQAtEDAKLRLEV--------NMQALKAQFERDLQARDEQGEEKRRQ 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1321 LEEEtkaknalahavqsarhdcdlLRE-QYEEEQEAKaelQRGMSKAnsevaqwrtkyetdaihrteeleeAKKKLAQRL 1399
Cdd:pfam01576 747 LVKQ--------------------VRElEAELEDERK---QRAQAVA------------------------AKKKLELDL 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1400 QDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAAcialdkkqrnfdkvlaewkhkYEETQAELEASQKESRSL 1479
Cdd:pfam01576 780 KELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAS---------------------RDEILAQSKESEKKLKNL 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1480 STELFKVKnayeetlDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGK 1559
Cdd:pfam01576 839 EAELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDR 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1560 ILRIQLELNQVKSEI--DRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALriKKKMEGDLNEMEIQLNHANRQ 1637
Cdd:pfam01576 912 LRKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSS--IAALEAKIAQLEEQLEQESRE 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1638 ASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQL 1717
Cdd:pfam01576 990 RQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNES 1069
|
890
....*....|
gi 826320982 1718 LHTQNTSLIN 1727
Cdd:pfam01576 1070 MNREVSTLKS 1079
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1210-1887 |
5.92e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1210 DNLQRVKQKLEKEKSELKMEIddlasnmetvsKAKGNFEKMCRTLEDQLSEVKtkeeeqqRLINELSAQKARLHTESGEF 1289
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKELEEVL-------REINEISSELPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1290 SRQLDEKEALVSQlsrgkqaftqqIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQ--RGMSKAN 1367
Cdd:PRK03918 227 EKEVKELEELKEE-----------IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1368 SEVAQWRTKYETdaihRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIdversnaaciaLDKK 1447
Cdd:PRK03918 296 IKLSEFYEEYLD----ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----------LEER 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1448 QRNFDKVLAEwkhkyeetQAELEASQKESRSLSTElfKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHE 1527
Cdd:PRK03918 361 HELYEEAKAK--------KEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1528 LEKVKKQIDQEKSELqasleeaeaSLEHEEGKILRIQLELNQVKSEIdRKIAEKDEEIdqlkRNHLRVVESmqstldaeI 1607
Cdd:PRK03918 431 LKKAKGKCPVCGREL---------TEEHRKELLEEYTAELKRIEKEL-KEIEEKERKL----RKELRELEK--------V 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1608 RSRNDALRIKKKMEGDLNEMEIQLNHAN----RQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANlm 1683
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNleelEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD-- 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1684 qaEVEELRASLEQTERSRKMAEQELLDasERVQLLHTQNTSLIntkkkletdishiqgEMEDIVQEARNAEEKAKKAITD 1763
Cdd:PRK03918 567 --ELEEELAELLKELEELGFESVEELE--ERLKELEPFYNEYL---------------ELKDAEKELEREEKELKKLEEE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1764 AAMMAEELkkeQDTSAHLERMKKNMEQtvkdLQHRLDEAEQlalkggkkqiQKLEARVRELENEVEGEQRRNVEAVKSLR 1843
Cdd:PRK03918 628 LDKAFEEL---AETEKRLEELRKELEE----LEKKYSEEEY----------EELREEYLELSRELAGLRAELEELEKRRE 690
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 826320982 1844 KHERRVKELTYQTEEDRKNVLRLQDL------VDKLQTKVKAYKRQAEEA 1887
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLekalerVEELREKVKKYKALLKER 740
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1039-1932 |
6.01e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 81.25 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1039 SLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKiEDEQAVGMQLQKKIKELQARTE 1118
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1119 ELEEEIEaeraSRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREA-EFQKMRRDLEEATLQHEATAAALRKK 1197
Cdd:TIGR00606 266 KLDNEIK----ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1198 HADSVAELGE-----QIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQ-------LSEVKTKE 1265
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktaaqlCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1266 EEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLL 1345
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1346 REQYEeeQEAKAELQRGMSKANSEVAQwrTKYETDAIHRTEELEEAKKKLAQRLQDAE-EHVEAVNSKCA------SLEK 1418
Cdd:TIGR00606 502 EVKSL--QNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkkQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1419 TKQRLQNEV---EDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESrslsTELFKVKNAYEETLD 1495
Cdd:TIGR00606 578 WLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEE----SDLERLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1496 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQV----- 1570
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglap 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1571 --KSEIDRKIAEKDEEIDQLK---------RNHLRVVESMQSTLDAEIRSRNDALR-----IKKKMEGDLNEMEIQLNHA 1634
Cdd:TIGR00606 734 grQSIIDLKEKEIPELRNKLQkvnrdiqrlKNDIEEQETLLGTIMPEEESAKVCLTdvtimERFQMELKDVERKIAQQAA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1635 NRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEEL---RASLEQTERSRKMAEQELLDA 1711
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQLVEL 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1712 SERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEArnaEEKAKKAITDAAMMAEELKK--------EQDTSAHLER 1783
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK---ETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDD 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1784 MKKNMEQTVKDLQHRLDEAEQlalkgGKKQIQKlEARVRELENEVEGEQRRNVEAVKSLRKHERRVKEL-----TYQTEE 1858
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHLKEM 1044
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1859 DRKNVLRLQDLVDKLQTKVKAYKR-------QAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHT 1931
Cdd:TIGR00606 1045 GQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYY 1124
|
.
gi 826320982 1932 K 1932
Cdd:TIGR00606 1125 K 1125
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
918-1823 |
6.91e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.79 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 918 EAKIKEATERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenkvknlteemagLDENIAKLAK 996
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL---------------NEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 997 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQ 1076
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1077 QLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEag 1156
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1157 gatsaqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsvaELGEQIDNLQRvkqKLEKEKSELKMEIDDLASN 1236
Cdd:pfam02463 403 ----------EEKEAQLLLELARQLEDLLKEEKKEELEILE------EEEESIELKQG---KLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1237 METVSKAKGNFEkmcrtledqlSEVKTKEEEQQRLINELSAQKARLHTESGEFSRqLDEKEALVSQLSRGKqaFTQQIEE 1316
Cdd:pfam02463 464 ELELKKSEDLLK----------ETQLVKLQEQLELLLSRQKLEERSQKESKARSG-LKVLLALIKDGVGGR--IISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1317 LKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLa 1396
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1397 QRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNaacIALDKKQRNFDKVLAEWKHKYEETQAELEASQKES 1476
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG---VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1477 RSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEkselqaSLEEAEASLEHE 1556
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEE------EEEEEKSRLKKE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1557 EGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEirsrndalriKKKMEGDLNEMEIQLNHANR 1636
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL----------KEEAELLEEEQLLIEQEEKI 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1637 QASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQ 1716
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1717 LLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAItdaamMAEELKKEQDTSAHLERMKKN----MEQTV 1792
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-----EEEEERNKRLLLAKEELGKVNlmaiEEFEE 985
|
890 900 910
....*....|....*....|....*....|.
gi 826320982 1793 KDLQHRLDEAEQLALKGGKKQIQKLEARVRE 1823
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1312-1911 |
1.14e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.34 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1312 QQIEELKRQLEEETKAKNALAHAVQSArhdcdllrEQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEE---- 1387
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELA--------ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAelar 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1388 LEEAKKKLAQRLQDAEEHVEAVNSKCASLE-KTKQRLQNEVEDLMIDVERsnaaciaLDKKQRNFDKVLAEWKHKYEETQ 1466
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEE-------RERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1467 AELEASQKESRSLSTELFKVKNAYEETLDQLETLKREnknLQQEISDLTEQIAEggkhiheLEKVKKQIDQEKSELQASL 1546
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIAS-------LERRKSNIPARLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1547 EEAeASLEHEEgkiLRIQLELNQVKSEID--RKIAEK------------DEEIDQLKR----NHLR---VVESMQSTLDA 1605
Cdd:COG4913 450 AEA-LGLDEAE---LPFVGELIEVRPEEErwRGAIERvlggfaltllvpPEHYAAALRwvnrLHLRgrlVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1606 EIRSRNDALRIKKKMEGDLN------EMEIQlNHANRQASEAIRNLRNTQ-GVLKDTQLH-------LDDAIRSQDDL-- 1669
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHpfrawlEAELG-RRFDYVCVDSPEELRRHPrAITRAGQVKgngtrheKDDRRRIRSRYvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1670 ----KEQLAMVERRANLMQAEVEELRASLEQTERSRKmAEQELLDASERVQllhTQNTSLINTkKKLETDISHIQGEMED 1745
Cdd:COG4913 605 gfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLA---EYSWDEIDV-ASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1746 IvqearnaeEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELE 1825
Cdd:COG4913 680 L--------DASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEE--------ELDELQDRLEAAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1826 NEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDR-KNVLRLQDLVDKLQTKVKAYKRQ--AEEAEEQSNVN-----LAR 1897
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIdALRARLNRAEEELERAMRAFNREwpAETADLDADLEslpeyLAL 820
|
650
....*....|....*
gi 826320982 1898 FRKIQHE-LEEAEER 1911
Cdd:COG4913 821 LDRLEEDgLPEYEER 835
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1257-1923 |
1.51e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.83 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1257 QLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQ-----------------LSRGKQAFTQQIEELKR 1319
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqaetelcaeaeemrarLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1320 QLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVaqwrTKYETDAI---HRTEELEEAKKKLA 1396
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKI----KKLEEDILlleDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1397 QRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKES 1476
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1477 RSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHE 1556
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1557 EGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANR 1636
Cdd:pfam01576 319 QELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1637 QASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMverranlMQAEVEELRASLEQTE----RSRK---MAEQELL 1709
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAEgkniKLSKdvsSLESQLQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1710 DASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNME 1789
Cdd:pfam01576 472 DTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1790 QTVKDLQHRLDEAEQLALKggkkqIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELtyqTEEDRKNVLRLQDL 1869
Cdd:pfam01576 552 RELEALTQQLEEKAAAYDK-----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQM---LAEEKAISARYAEE 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1870 VDKlqtkvkaykrqaeeAEEQSNVNLARFRKIQHELEEAEERADIAESQVNKLR 1923
Cdd:pfam01576 624 RDR--------------AEAEAREKETRALSLARALEEALEAKEELERTNKQLR 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1384-1923 |
1.86e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1384 RTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKqrlqNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYE 1463
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1464 ETQaELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKqidqEKSELQ 1543
Cdd:PRK03918 277 ELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK----KLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1544 ASLEEAEASLEHEEgKILRIQLELNQVKSEIdrkiaeKDEEIDQLKRNhLRVVESMQSTLDAEIRSRNDALRIKKKMEGD 1623
Cdd:PRK03918 352 KRLEELEERHELYE-EAKAKKEELERLKKRL------TGLTPEKLEKE-LEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1624 LNEMEIQLNHANRQASEAIRNLrntqgvlkdtqlhlddairSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKM 1703
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGREL-------------------TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1704 AEQELLDASeRVQLLHTQNTSLINTKKKLEtdiSHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDtsahLER 1783
Cdd:PRK03918 485 LEKVLKKES-ELIKLKELAEQLKELEEKLK---KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1784 MKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEnEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNV 1863
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 826320982 1864 LRLQDLVDKLQTKVKAYKRQ--AEEAEEQSNVNLARFRKI---QHELEEAEERADIAESQVNKLR 1923
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKysEEEYEELREEYLELSRELaglRAELEELEKRREEIKKTLEKLK 700
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
837-1329 |
2.16e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.91 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 837 KIKPLLKSAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQ 916
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 917 LEAKIKEATERAEDEEEINAELT---AKKRKLEDECSELKKDIDDLELTLAKVE---------------------KEKHA 972
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsekqKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 973 TENKVKNLTEEMAGLDENIAKLAKEKKalQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLER 1052
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1053 AKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRA 1132
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1133 KAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQheataaalrkkhadsVAELGEQIDNL 1212
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE---------------LKSKEKELKKL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1213 QRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQL---------SEVKTKEEEQQRLINELSAQKARLH 1283
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLK 581
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 826320982 1284 TESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLeEETKAKN 1329
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL-EKAKKEN 626
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
2.48e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 68.61 E-value: 2.48e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 826320982 33 DAKTSVFVADPKESFVKATVQSREGGKVTAKTEGGSTVTVKDDQV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
912-1628 |
5.13e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 77.84 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 912 KTKIQLEAKIKEATERAEDEEEINAELTAkkRKLEDECSELKKDIddleltlakveKEKHATENKVKNLTEEMAGLDENI 991
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVS--LKLEEEIQENKDLI-----------KENNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 992 AKLAKEKkalqEAHQQTLDDLQaeedkvNTLTKAKTKLEQ-QVDDLEGSLEQEKKLRMDLERAKRklegdlkLAQESTMD 1070
Cdd:pfam05483 172 KKYEYER----EETRQVYMDLN------NNIEKMILAFEElRVQAENARLEMHFKLKEDHEKIQH-------LEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1071 IENDKQQLDEKL---KKKEFEMSNLQSKIEDEQAVGMQLQKKIKeLQARTEEleeeieaerasraKAEKQRSDLSRELEE 1147
Cdd:pfam05483 235 INDKEKQVSLLLiqiTEKENKMKDLTFLLEESRDKANQLEEKTK-LQDENLK-------------ELIEKKDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1148 ISERLEEaggATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAAlRKKHADSVAELGEQIDNLQRV----KQKLEKEK 1223
Cdd:pfam05483 301 IKMSLQR---SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-KAAHSFVVTEFEATTCSLEELlrteQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1224 SELK---MEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKT---KEEEQQRLINELSAQKARLHTESGEFSRQLDEKE 1297
Cdd:pfam05483 377 DQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1298 ALVSQLSRGKQAFTQQIEELKRQLEEEtKAKNALAHAvqsarhDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRtKY 1377
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKE-KLKNIELTA------HCDKLLLENKELTQEASDMTLELKKHQEDIINCK-KQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1378 ETDAIHRTEELEEAKKKLAQRLQDAEEHV----EAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDK 1453
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1454 VLAEWkhkYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDltEQIAEgGKHIHELEKVKK 1533
Cdd:pfam05483 609 NIEEL---HQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED--KKISE-EKLLEEVEKAKA 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1534 QIDqEKSELQaslEEAEASLEHeegKILRIQLELNQVKSEIDRKIAEKDEEIDqLKRNHLRVVESMQSTLDAEIRS-RND 1612
Cdd:pfam05483 683 IAD-EAVKLQ---KEIDKRCQH---KIAEMVALMEKHKHQYDKIIEERDSELG-LYKNKEQEQSSAKAALEIELSNiKAE 754
|
730
....*....|....*.
gi 826320982 1613 ALRIKKKMEGDLNEME 1628
Cdd:pfam05483 755 LLSLKKQLEIEKEEKE 770
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
841-1611 |
5.35e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.09 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 841 LLKSAETEKEMANMKEEFEKA----------KEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQL 910
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENkeeekekklqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 911 IKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEN 990
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE----QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 991 IAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQestmd 1070
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE----- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1071 iendkQQLDEKLKKKEFEMSNLQSKIEDEQAV---GMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEE 1147
Cdd:pfam02463 485 -----QLELLLSRQKLEERSQKESKARSGLKVllaLIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1148 ISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELK 1227
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1228 MEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKA--RLHTESGEFSRQLDEK-------EA 1298
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEeiLRRQLEIKKKEQREKEelkklklEA 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1299 LVSQLSRGKQAFTQQIEELKRQLEEET-KAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKY 1377
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1378 ETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAAC-IALDKKQRNFDKVLA 1456
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEItKEELLQELLLKEEEL 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1457 EWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTE-------QIAEGGKHIHELE 1529
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEllleeadEKEKEENNKEEEE 959
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1530 KVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRS 1609
Cdd:pfam02463 960 ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFY 1039
|
..
gi 826320982 1610 RN 1611
Cdd:pfam02463 1040 LE 1041
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
877-1588 |
6.31e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 77.70 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 877 EKMVTLMQEKNDLQLQVQAEADslaDAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTaKKRKLEDECSELKKdi 956
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQ-- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 957 ddlELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDl 1036
Cdd:TIGR00618 261 ---LLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1037 EGSLEQEKKLRMDLERAKRKLEgDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQkkikELQAR 1116
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIR-DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ----REQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1117 TEELEEEIEAERASRAKAEKQRsdlsrELEEISERLEEAGGATSAQIEmnKKREAEFQKMRRDLEEATlQHEATAAALRK 1196
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQ-----ELQQRYAELCAAAITCTAQCE--KLEKIHLQESAQSLKERE-QQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1197 KHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLasnmetvskakGNFEKMCRTLEDQLSEVKTKEEEQQRLINELS 1276
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI-----------DNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1277 AQKARLHTESGEFSRQLDEKEALVSQLSRGKQAF---TQQIEELKRQLEEETKAKNALAhavqsarhdcDLLREQYEEEQ 1353
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLA----------CEQHALLRKLQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1354 EAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLmid 1433
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML--- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1434 vERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEA-------SQKESRSLSTELFKVK-NAYEETLDQLETLKRENK 1505
Cdd:TIGR00618 700 -AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqSLKELMHQARTVLKARtEAHFNNNEEVTAALQTGA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1506 NLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEI 1585
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
...
gi 826320982 1586 DQL 1588
Cdd:TIGR00618 859 KQL 861
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1361 |
2.22e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 842 LKSAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQL------QVQAEADSL----ADAEERCDQLI 911
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleeheERREELETLeaeiEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 912 KTKIQLEAKIKEATERAEDEEEINAELTAK-------KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEM 984
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 985 AGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDD----LEGSLEQEKKLRMDLERAKRK---L 1057
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREReaeL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1058 EGDLKLAQESTmdieNDKQQLDEKLK----KKEFEMSNLQSKIEDEQAVGMQLQKKIKELqaRTEELEEEIEAERASRA- 1132
Cdd:PRK02224 432 EATLRTARERV----EEAEALLEAGKcpecGQPVEGSPHVETIEEDRERVEELEAELEDL--EEEVEEVEERLERAEDLv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1133 KAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaelgEQIDNL 1212
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAAELEAEAEEKREAAAEAE-----------EEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1213 QRVKQKLEKEKSELKMEIDDLasnmetvskakgnfekmcRTLEDQLSEVKTKEEEQQRLiNELSAQKARLHTESGEF--- 1289
Cdd:PRK02224 571 REEVAELNSKLAELKERIESL------------------ERIRTLLAAIADAEDEIERL-REKREALAELNDERRERlae 631
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1290 ----SRQLDEK--EALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQR 1361
Cdd:PRK02224 632 krerKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1416-1925 |
3.73e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.15 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1416 LEKTKQRLQNEVEDLMIDVERSNAaciaLDKKQRNF-DKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETL 1494
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNE----LHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1495 DQLETLKRENKNLQQEISDLTEQIaeggkhiHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLElnQVKSEI 1574
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQL-------RKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR--SLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1575 DRKIAEKDEEIDQLKrNHLRVVESMQSTLDAEIRSRNDAL--RIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQgvl 1652
Cdd:pfam15921 223 SKILRELDTEISYLK-GRIFPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ--- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1653 kdTQLHLddairSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERsrkMAEQELLDASERVQLLHTQntslintkkkl 1732
Cdd:pfam15921 299 --SQLEI-----IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR---MYEDKIEELEKQLVLANSE----------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1733 etdISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlalkggkk 1812
Cdd:pfam15921 358 ---LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM-------- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1813 QIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKnvlRLQDLVDKLQTkvkayKRQAEEAEEQSN 1892
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEELTA-----KKMTLESSERTV 498
|
490 500 510
....*....|....*....|....*....|...
gi 826320982 1893 VNLARfrkiqhELEEAEERADIAESQVNKLRVK 1925
Cdd:pfam15921 499 SDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
869-1448 |
5.37e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.77 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 869 EAKRKELEEKMVTLMQEKNDLQLQVQAEAD----------SLADAEERCDQLIKTKIQLEAK------IKEATERAEDEE 932
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLISEHEveitgltekaSSARSQANSIQSQLEIIQEQARnqnsmyMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 933 EINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLD 1010
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKLLADLHKREKELSLEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1011 dlqaeEDKVNTLTkaktkleqqVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLkkkefemS 1090
Cdd:pfam15921 406 -----RDTGNSIT---------IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV-------S 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1091 NLQSKIEDEQAVgmqLQKKIKELQARteeleeeieaeRASRAKAEKQRSDLSRELEEISERLEeaggATSAQIEMNKKRE 1170
Cdd:pfam15921 465 SLTAQLESTKEM---LRKVVEELTAK-----------KMTLESSERTVSDLTASLQEKERAIE----ATNAEITKLRSRV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1171 ----AEFQKMRRDLEE-ATLQHEATAAALRKKHADSVAE-LGEQIDNLQ-------RVKQKLEKEKSELKMEIDDLASNM 1237
Cdd:pfam15921 527 dlklQELQHLKNEGDHlRNVQTECEALKLQMAEKDKVIEiLRQQIENMTqlvgqhgRTAGAMQVEKAQLEKEINDRRLEL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1238 ETVSKAKGNFEKMCRTLEDQLSEVktkEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSrgkqAFTQQIEEL 1317
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDL---ELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELN----SLSEDYEVL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1318 KRQL----EEETKAKNALAHAVQSARHDCDLLREQYEEEQ-------------EAKAELQRGMSKANSEVAQWRTKYETD 1380
Cdd:pfam15921 680 KRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgmQKQITAKRGQIDALQSKIQFLEEAMTN 759
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1381 AIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSN---AACIALDKKQ 1448
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfAECQDIIQRQ 830
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
894-1772 |
1.49e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 73.16 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 894 QAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHAT 973
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 974 ENKVKNLTEEMAGLDENIAKLAKEKKALQEAH-----QQTLDDLQAEEDKVNTLTKAKTKLEQQ----VDDLEGSLEQEK 1044
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKtellvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1045 KLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAV----GMQLQKKIKELQARTEEL 1120
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIlekkQEELKFVIKELQQLEGSS 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1121 EEEIEAERASR------AKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATA-AA 1193
Cdd:TIGR00606 471 DRILELDQELRkaerelSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKdEQ 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1194 LRKKHADSVAELGEQIDNLQRVKQ------KLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTK--- 1264
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfd 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1265 -------EEEQQRLINEL---SAQKARLHTESGEFSRQLD---------------------EKEALVSQLSRGKQAFTQQ 1313
Cdd:TIGR00606 631 vcgsqdeESDLERLKEEIeksSKQRAMLAGATAVYSQFITqltdenqsccpvcqrvfqteaELQEFISDLQSKLRLAPDK 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1314 IEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETdaIHRTEELEE--- 1390
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT--IMPEEESAKvcl 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1391 ----AKKKLAQRLQDAEEHVEAVNSKCAS--LEKTKQRLQNEVEDlmidversnaacialdkKQRNFDKVLAewkhKYEE 1464
Cdd:TIGR00606 789 tdvtIMERFQMELKDVERKIAQQAAKLQGsdLDRTVQQVNQEKQE-----------------KQHELDTVVS----KIEL 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1465 TQAELEASQKESRSLSTELFKVKN---AYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSE 1541
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1542 LQASleeaeaslEHEEGKIlrIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKME 1621
Cdd:TIGR00606 928 LISS--------KETSNKK--AQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKIN 997
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1622 GDLNEMEIQLNHANRQASEAIRNLrntqgvlkdTQLHLDDAIRsqdDLKEQLAMVERRANLMQAeveelrasLEQTERSR 1701
Cdd:TIGR00606 998 EDMRLMRQDIDTQKIQERWLQDNL---------TLRKRENELK---EVEEELKQHLKEMGQMQV--------LQMKQEHQ 1057
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1702 KMAEQELLDASERVQLLHTQntslintkKKLETDISHIQGEMEDivQEARNAEEKAKKAITDAAMMAEELK 1772
Cdd:TIGR00606 1058 KLEENIDLIKRNHVLALGRQ--------KGYEKEIKHFKKELRE--PQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1273 |
2.02e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 837 KIKPLLKSAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQ 916
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 917 LEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatENKVKnlTEEMAGLDENIAKLAK 996
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIK--AAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 997 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDiENDKQ 1076
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKK 1757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1077 QLDEKlkKKEFEMSNLQSKIEDEQAVGMQLQKKikelqarteeleeeieaERASRAKAEKQRSDLSRELEEISERLEEAG 1156
Cdd:PTZ00121 1758 KIAHL--KKEEEKKAEEIRKEKEAVIEEELDEE-----------------DEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1157 GATSAQIEM---NKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDL 1233
Cdd:PTZ00121 1819 LVINDSKEMedsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDI 1898
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 826320982 1234 ASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLIN 1273
Cdd:PTZ00121 1899 EREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
885-1519 |
2.06e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 72.95 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 885 EKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEA---KIKEATERAEDEEEINAELTAKKRkledecSELKKDIDDLEL 961
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHlhfGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 962 TLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAE-----------EDKVNTLTKAKTKL- 1029
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTAKYNRRr 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1030 ----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlAQESTMDIENDKQQLDEKLKKKEFE--MSNLQSKIEDEQAVG 1103
Cdd:pfam12128 382 skikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGELKLRLNQATATP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1104 ---MQLQKKIKELQ-ARTEELEEEIEAERAS--RAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMR 1177
Cdd:pfam12128 461 ellLQLENFDERIErAREEQEAANAEVERLQseLRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1178 R----DLEEATLQHEATAAALRKK-HADSVAELGEQIDNL-------------------QRVKQKLEKEKSELKMEIDDL 1233
Cdd:pfam12128 541 RkeapDWEQSIGKVISPELLHRTDlDPEVWDGSVGGELNLygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1234 ASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEK----EALVSQLSRGKQA 1309
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERlnslEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1310 FTQQIeelKRQLEEETKAKNALAHAVQSARHD-CDLLREQYEEEQE-AKAELQRGMSKANSEVAQWRTKYETDAihrteE 1387
Cdd:pfam12128 701 WLEEQ---KEQKREARTEKQAYWQVVEGALDAqLALLKAAIAARRSgAKAELKALETWYKRDLASLGVDPDVIA-----K 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1388 LEEAKKKLAQRLQDAEEHVEAVNSKCASLEKT----KQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYE 1463
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEVLRYFDWYQETwlqrRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE 852
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1464 ETQAELEASQKESRSLSTELFKVKNAYE---------ETLDQLETLKRENKNL----QQEISDLTEQIA 1519
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLATLKEDANseqaqgsigERLAQLEDLKLKRDYLsesvKKYVEHFKNVIA 921
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
836-1256 |
2.16e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 836 FKIKPLLKSAETEKEMANMKEEFEKAKEELAKSEAKR---KELEEKMVTLMQEKNDLQLQVQAEADSLADAEE----RCD 908
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 909 QLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATENKVKNLTEE 983
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKELLEEYTAE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 984 MAGLDENIAKLAKEKKALqEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEG----SLEQEKKLRMDLERAKRKLEG 1059
Cdd:PRK03918 461 LKRIEKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1060 DLKLAQ---ESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGM-QLQKKIKELQARTEELEEEIEAERASRAKaE 1135
Cdd:PRK03918 540 EIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPFYNEYLELKDAEKELERE-E 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1136 KQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATaaALRKKHADSVAELGEqidnlqrv 1215
Cdd:PRK03918 619 KELKKLEEELDKAFEELAE----TEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEE-------- 684
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 826320982 1216 kqkLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLED 1256
Cdd:PRK03918 685 ---LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1200-1873 |
2.73e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1200 DSVAELGEQIDNLQRVKQKLEKEKSELKM--EIDDLASNMETVSKAKGNFEKMCRTLEDQLSEvkTKEEEQQRLINELSA 1277
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1278 QKARLHTESGEFSRQLDEKEALVSQLSRGKQAF-TQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAK 1356
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1357 AELQRgmskansEVAQWRTKYETdaihRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTK---------------Q 1421
Cdd:COG4913 383 AALRA-------EAAALLEALEE----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparllalrdalaE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1422 RLQNEVEDL-----MIDVE--------------RSNAACIALDkkQRNFDKVLaEW-----------KHKYEETQAELEA 1471
Cdd:COG4913 452 ALGLDEAELpfvgeLIEVRpeeerwrgaiervlGGFALTLLVP--PEHYAAAL-RWvnrlhlrgrlvYERVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1472 SQKESRSLSTELFKVKNAYEETLDQL-------------ETLKRENKNLQQE--ISDLTEQIAEGGKH------------ 1524
Cdd:COG4913 529 PRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAITRAgqVKGNGTRHEKDDRRrirsryvlgfdn 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1525 ---IHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID-----RKIAEKDEEIDQLKRNHlrvv 1596
Cdd:COG4913 609 rakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLDASS---- 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1597 esmqstldaeirsrndalrikkkmeGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMV 1676
Cdd:COG4913 685 -------------------------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1677 ERRANL-MQAEVEELRASLEQTERSRKMAEQelldASERVQllhTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEE 1755
Cdd:COG4913 740 EDLARLeLRALLEERFAAALGDAVERELREN----LEERID---ALRARLNRAEEELERAMRAFNREWPAETADLDADLE 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1756 kakkAITDAAMMAEELkKEQDTSAHLERMK----KNMEQTVKDLQHRLDEAEQLAlkggKKQIQKLEARVRELE-NevEG 1830
Cdd:COG4913 813 ----SLPEYLALLDRL-EEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfG--PG 881
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1831 E------QRRNVEAVKSLRKHERRVKELTYQTEED--RKNVLRLQDLVDKL 1873
Cdd:COG4913 882 RylrleaRPRPDPEVREFRQELRAVTSGASLFDEElsEARFAALKRLIERL 932
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1257-1900 |
5.10e-12 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 71.32 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1257 QLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQL-------DEKEALVSQLSrGKQAFTQQIEELK-RQLEE-ETKA 1327
Cdd:pfam07111 71 QLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAvaekagqAEAEGLRAALA-GAEMVRKNLEEGSqRELEEiQRLH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1328 KNALAHAVQSARHDCDLLREQYE--EEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQD--AE 1403
Cdd:pfam07111 150 QEQLSSLTQAHEEALSSLTSKAEglEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKyvGE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1404 EHVEAVNSKCASLEK-----TKQRLQNEVEDLMIDVErsnaaciALDKKQRNFDKVLA----EWKHKYEETQAELEASQK 1474
Cdd:pfam07111 230 QVPPEVHSQTWELERqelldTMQHLQEDRADLQATVE-------LLQVRVQSLTHMLAlqeeELTRKIQPSDSLEPEFPK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1475 ESRSLstelfkVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEggkhihELEKVKKQiDQEKSELQASLEEAEASLE 1554
Cdd:pfam07111 303 KCRSL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE------LQEQVTSQ-SQEQAILQRALQDKAAEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1555 HEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKrnhlRVVESMQSTLDaeirsrndalRIKKKMeGDLNEMEIQLNHA 1634
Cdd:pfam07111 370 VERMSAKGLQMELSRAQEARRRQQQQTASAEEQLK----FVVNAMSSTQI----------WLETTM-TRVEQAVARIPSL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1635 NRQASEAIRNLRNTQGVLKD----TQLHLDDAIRSQD------DLKEQLAMVERRANLMQAEVeELRASLEQTERSRKMA 1704
Cdd:pfam07111 435 SNRLSYAVRKVHTIKGLMARkvalAQLRQESCPPPPPappvdaDLSLELEQLREERNRLDAEL-QLSAHLIQQEVGRARE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1705 EQElldaSERVQllhtqntsLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQdtsahlERM 1784
Cdd:pfam07111 514 QGE----AERQQ--------LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQ------EIY 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1785 KKNMEQTVKDLQHRLDEaeqlalkggkkQIQKLEARVRElenevegEQRRNVEAVKSLRKHERRVKeltyQTEEDRKNVL 1864
Cdd:pfam07111 576 GQALQEKVAEVETRLRE-----------QLSDTKRRLNE-------ARREQAKAVVSLRQIQHRAT----QEKERNQELR 633
|
650 660 670
....*....|....*....|....*....|....*.
gi 826320982 1865 RLQDLVDKLQTKVKAykRQAEEAEEQSNVNLARFRK 1900
Cdd:pfam07111 634 RLQDEARKEEGQRLA--RRVQELERDKNLMLATLQQ 667
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
837-1271 |
5.77e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 837 KIKPLLKSAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQaeadSLADAEERCDQLIKTKIQ 916
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 917 LEAKIKEATERAEDEEEINAeLTAKKRKLEDECSELkkDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAK 996
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 997 EKKALQEAHQQ--TLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTM--DIE 1072
Cdd:PRK03918 427 AIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1073 NDKQQLD----EKLKKKEFEMSNLQSK---IEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRE- 1144
Cdd:PRK03918 507 ELEEKLKkynlEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEs 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1145 LEEISERLEEAGGATSAQIEM-NKKREAEFQKMRRDLEEATLqhEATAAALRKKHADsVAELGEQIDNLQRV-----KQK 1218
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELkDAEKELEREEKELKKLEEEL--DKAFEELAETEKR-LEELRKELEELEKKyseeeYEE 663
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 826320982 1219 LEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRL 1271
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1050-1590 |
6.88e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 71.09 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1050 LERAKRKLEGDLKLAQESTMDIENdkqqLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERA 1129
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1130 SR-----------------AKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1192
Cdd:PRK01156 240 ALnelssledmknryeseiKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1193 ALRKKHADSVAELGEQIDNLQRVKQKleKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLI 1272
Cdd:PRK01156 320 EINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1273 NELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEE 1352
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1353 ----QEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQ-------------RLQDAEEHVEAVNSKCAS 1415
Cdd:PRK01156 478 ksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledikikinELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1416 LEKTKQRLQNEvEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLD 1495
Cdd:PRK01156 558 LKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1496 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVkSEID 1575
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI-NELS 715
|
570
....*....|....*
gi 826320982 1576 RKIAEKDEEIDQLKR 1590
Cdd:PRK01156 716 DRINDINETLESMKK 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1382-1937 |
3.63e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1382 IHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKhK 1461
Cdd:PRK03918 154 ILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-E 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1462 YEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEqIAEGGKHIHELEKVKKQIDQEKSE 1541
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1542 LQASLEEAEASLEHEEGKILRIQlELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEirsrndalRIKKKME 1621
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE--------RLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1622 G----DLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIrsqddlkEQLAMVERRANLMQAEVEElrasleqT 1697
Cdd:PRK03918 383 GltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-------EELKKAKGKCPVCGRELTE-------E 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1698 ERSRKMAE--QELLDASERVQLLHTQNTSLINTKKKLETDISHIQG--EMEDIVQEARNAEEKAKKaitdaaMMAEELKK 1773
Cdd:PRK03918 449 HRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKK------YNLEELEK 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1774 EQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLalkggKKQIQKLEARVRELENEV-EGEQRRNVEAVKSLRKHERRVKEL 1852
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL-----KKKLAELEKKLDELEEELaELLKELEELGFESVEELEERLKEL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1853 tyqtEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEeqsnvnlarfrKIQHELEEAEERADIAESQVNKLRVKSREVHTK 1932
Cdd:PRK03918 598 ----EPFYNEYLELKDAEKELEREEKELKKLEEELD-----------KAFEELAETEKRLEELRKELEELEKKYSEEEYE 662
|
....*
gi 826320982 1933 IISEE 1937
Cdd:PRK03918 663 ELREE 667
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1098 |
4.60e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 845 AETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDL-----QLQVQAEADSLADAEERCDQLIKTKIQLEA 919
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 920 KIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKK 999
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1000 ALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEG-------------SLEQEKKLRMDLERAKRKLEGDLKLAQE 1066
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
250 260 270
....*....|....*....|....*....|..
gi 826320982 1067 STMDIENDKQQLDEKLKKKEFEMSNLQSKIED 1098
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1213-1890 |
5.13e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.74 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1213 QRVKQKLEKEKSELK---MEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEF 1289
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1290 SRQLDEKEalvSQLSRGKQAFTQQIEELKRQLEEETKAKNALAhavqSARHDCDLLREQYEEEQEAKAELQRGMSKANSE 1369
Cdd:TIGR04523 116 KEQKNKLE---VELNKLEKQKKENKKNIDKFLTEIKKKEKELE----KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1370 VAQWRTKYetdaiHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQR 1449
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1450 NFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLD-----QLETLKRENKNLQQEISDLTEQIAEGGKH 1524
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelksELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1525 IHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEI---DRKIaEKDEEIDQLKRNHLRVVESMQS 1601
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndlESKI-QNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1602 TLDAEIRsrndalrikkkmegDLNEMEIQLNhanrqasEAIRNLRNTQGVLKDTQLHLDdaiRSQDDLKEQLAMVERRAN 1681
Cdd:TIGR04523 423 LLEKEIE--------------RLKETIIKNN-------SEIKDLTNQDSVKELIIKNLD---NTRESLETQLKVLSRSIN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1682 LMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIvqearnaEEKAKKai 1761
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL-------EDELNK-- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1762 tdaamMAEELKKEQdtsahLERMKKNMEQTVKDLQHrldeaeqlalkggkkQIQKLEARVRELENEVEGEQRRNVEAVKS 1841
Cdd:TIGR04523 550 -----DDFELKKEN-----LEKEIDEKNKEIEELKQ---------------TQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 826320982 1842 LRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQ 1890
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
873-1876 |
5.83e-11 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 68.15 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 873 KELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSEl 952
Cdd:TIGR01612 557 KKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNNAY- 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 953 kkdIDDL-ELTLAKVEKEKHATENKVKNLTEEMAGLDE-NIAKLAKEKKALQEAhqqtlDDLQAEEDKVNtLTKAKTKLE 1030
Cdd:TIGR01612 636 ---IDELaKISPYQVPEHLKNKDKIYSTIKSELSKIYEdDIDALYNELSSIVKE-----NAIDNTEDKAK-LDDLKSKID 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1031 QQVDDLEGSLEQEKKLRM-DLERAKRKLEGDL-KLAQESTMDIENDKQQLDEKLKKKEFEMSNlqsKIEDEQAVGMQLQK 1108
Cdd:TIGR01612 707 KEYDKIQNMETATVELHLsNIENKKNELLDIIvEIKKHIHGEINKDLNKILEDFKNKEKELSN---KINDYAKEKDELNK 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1109 ---KIKELQARTEELEEEIEaeraSRAKAEKQRSDLSRE-LEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEAT 1184
Cdd:TIGR01612 784 yksKISEIKNHYNDQINIDN----IKDEDAKQNYDKSKEyIKTISIKEDE----IFKIINEMKFMKDDFLNKVDKFINFE 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1185 LQHEATAAALRKKHADSVAELGEQI--DNLQRVKQKLEKEKS---ELKMEIDDLASNMETVSKAKGnFEKMCRTLEDQLS 1259
Cdd:TIGR01612 856 NNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSlinEINKSIEEEYQNINTLKKVDE-YIKICENTKESIE 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1260 EVKTKeeeqQRLINELSAQKARLHTESGEFSRQLDEK--EALVSQLSRGKQAFTQ-QIEELKRQLEEETKAKNALAHAVQ 1336
Cdd:TIGR01612 935 KFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfdNTLIDKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANLG 1010
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1337 SARHdcDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQdaEEHVEAVNSKCASL 1416
Cdd:TIGR01612 1011 KNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLN--KEILEEAEINITNF 1086
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1417 EKTKQRLQ----------------NEVEDLMIDVErsnaaciALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLS 1480
Cdd:TIGR01612 1087 NEIKEKLKhynfddfgkeenikyaDEINKIKDDIK-------NLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVA 1159
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1481 TELFKVKN--AYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVK---------------KQIDQEKSELQ 1543
Cdd:TIGR01612 1160 DKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKginlsygknlgklflEKIDEEKKKSE 1239
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1544 ASLEEAEASLEheegkilriqlELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVeSMQSTLDAEIRSRNDALRIKkkmegD 1623
Cdd:TIGR01612 1240 HMIKAMEAYIE-----------DLDEIKEKSPEIENEMGIEMDIKAEMETFNI-SHDDDKDHHIISKKHDENIS-----D 1302
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1624 LNEMEIQLNHANRQASeairnlrNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAE-----VEELRASLEQTE 1698
Cdd:TIGR01612 1303 IREKSLKIIEDFSEES-------DINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNkikkiIDEVKEYTKEIE 1375
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1699 RSRKMAEQElLDASERVQLLHTQNTSLINTKKKLETDI----------------SHIQGEMEDIVQEARNAEE------- 1755
Cdd:TIGR01612 1376 ENNKNIKDE-LDKSEKLIKKIKDDINLEECKSKIESTLddkdidecikkikelkNHILSEESNIDTYFKNADEnnenvll 1454
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1756 ------------------KAKKAITDAAMMAEELKKEQDTS-----------AHLERMKKNMEQTVKDLQHRLDEAEQLA 1806
Cdd:TIGR01612 1455 lfkniemadnksqhilkiKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEKNKELFEQYKKDVTELLNKYSALA 1534
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1807 LKGG----KKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTK 1876
Cdd:TIGR01612 1535 IKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENK 1608
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1076-1698 |
1.16e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.17 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1076 QQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARteeleeeieaerasrakaekQRSDLSRELEEISERLEEA 1155
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE--------------------LNQLLRTLDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1156 GGATSAQIEMNKKREAEFQKMRRDLEeATLQHEATAAALRKKHADSV--------AELGEQIDNLQRVKQKLE----KEK 1223
Cdd:pfam12128 307 NGELSAADAAVAKDRSELEALEDQHG-AFLDADIETAAADQEQLPSWqselenleERLKALTGKHQDVTAKYNrrrsKIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1224 SELKMEIDDLASNMETVSKAK--------GNFEKMCRTLEDQLSEVKTK-EEEQQRLINELSAQKARLHTESGEfSRQLD 1294
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARdrqlavaeDDLQALESELREQLEAGKLEfNEEEYRLKSRLGELKLRLNQATAT-PELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1295 EKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAEL--QRGMSKA--NSEV 1370
Cdd:pfam12128 465 QLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpQAGTLLHflRKEA 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1371 AQWRtkyetDAIHRTeeleeAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNevedlmIDVERSNAACIALDKKQRN 1450
Cdd:pfam12128 545 PDWE-----QSIGKV-----ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKR------IDVPEWAASEEELRERLDK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1451 FDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISD-LTEQIAEGGKHIHELE 1529
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSLE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1530 KVKKQIDQEkseLQASLEEA-EASLEHEEGKilriQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIR 1608
Cdd:pfam12128 689 AQLKQLDKK---HQAWLEEQkEQKREARTEK----QAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1609 SRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRN---LRNTQGVLKDT-QLHLDDAIRSQDDLKEQLAMVERRANLMQ 1684
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYfdwYQETWLQRRPRlATQLSNIERAISELQQQLARLIADTKLRR 841
|
650
....*....|....
gi 826320982 1685 AEVEELRASLEQTE 1698
Cdd:pfam12128 842 AKLEMERKASEKQQ 855
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1528-1932 |
1.23e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1528 LEKVKKQIDQEKS--------ELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKiAEKDEEIDQLKRNhlrvVESM 1599
Cdd:PRK02224 189 LDQLKAQIEEKEEkdlherlnGLESELAELDEEIERYEEQREQARETRDEADEVLEEH-EERREELETLEAE----IEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1600 QSTLDAEIRSRNDAlrikkkmegdlnemeiqlnhanrqaSEAIRNLRNTQGVLKD------TQLHLDDAirSQDDLKEQL 1673
Cdd:PRK02224 264 RETIAETEREREEL-------------------------AEEVRDLRERLEELEEerddllAEAGLDDA--DAEAVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1674 AMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNA 1753
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1754 EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLaLKGGK---------------------K 1812
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1813 QIQKLEARVRELENEVEGEQRRnVEAVKSLRKHERRVKELtyqtEEDRKNVlrlQDLVDKLQTKVKAYKRQAEEAEEQSN 1892
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEER-LERAEDLVEAEDRIERL----EERREDL---EELIAERRETIEEKRERAEELRERAA 547
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 826320982 1893 vnlarfrKIQHELEEAEERADIAESQVNKLRVKSREVHTK 1932
Cdd:PRK02224 548 -------ELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1154 |
1.44e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 846 ETEKEMANMKEEFEKAKEELAKSEAKRKELEEKmvtlmqekndlqlqVQAEADSLADAEERCDQLIKTKIQLEAKIkEAT 925
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE--------------IENVKSELKELEARIEELEEDLHKLEEAL-NDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 926 ERAEDEEEINaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAH 1005
Cdd:TIGR02169 785 EARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1006 QQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEStmdIENDKQQLD--EKLK 1083
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK---LEALEEELSeiEDPK 940
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1084 KKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEE 1154
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1502-1916 |
1.60e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1502 RENKNLQQEISDLTEQIAEGGK---HIHELEKVKKQIDQEKSELQASLEEAEASLEHEEgkILRIQLELNQVKSEIDRKI 1578
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEkeeEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1579 AEKDEEIDQLKRnhlrvvesmqstldaEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLrntqgvLKDTQLH 1658
Cdd:COG4717 142 AELPERLEELEE---------------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1659 LDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISH 1738
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1739 IQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQK 1816
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1817 LEARVRELENEV-----------EGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDK--LQTKVKAYKRQ 1883
Cdd:COG4717 361 EELQLEELEQEIaallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEE 440
|
410 420 430
....*....|....*....|....*....|...
gi 826320982 1884 AEEAEEQSNVNLARFRKIQHELEEAEERADIAE 1916
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
916-1162 |
2.90e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 916 QLEAKIKEATERAEDEEEInAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLA 995
Cdd:COG4942 18 QADAAAEAEAELEQLQQEI-AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 996 KEKKALQEAHQQTLDDLQaeedKVNTLTKAKTKLEQQ-VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEND 1074
Cdd:COG4942 97 AELEAQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1075 KQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTeeleeeieaerasrAKAEKQRSDLSRELEEISERLEE 1154
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL--------------AELQQEAEELEALIARLEAEAAA 238
|
....*...
gi 826320982 1155 AGGATSAQ 1162
Cdd:COG4942 239 AAERTPAA 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
869-1631 |
3.68e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 65.45 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 869 EAKRKELEEKMVTLMQEKNDLQlqvqaeaDSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEinaELTAKKRKLEDE 948
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQ-------SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE---ELKFVIKELQQL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 949 CSELKkDIDDLELTLAKVEKEKHATEN---------KVKNLTEEMAGLDENIAKLAKEKKAL---QEAHQQTLDDLQAEE 1016
Cdd:TIGR00606 467 EGSSD-RILELDQELRKAERELSKAEKnsltetlkkEVKSLQNEKADLDRKLRKLDQEMEQLnhhTTTRTQMEMLTKDKM 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1017 DKVNTLTKAKTKLEQQVDDLEGSLEQEKKLR---MDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQ 1093
Cdd:TIGR00606 546 DKDEQIRKIKSRHSDELTSLLGYFPNKKQLEdwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1094 SKIED---EQAVGMQLQKKIKELQarteeleeeieaerasraKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK--- 1167
Cdd:TIGR00606 626 DKLFDvcgSQDEESDLERLKEEIE------------------KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrvf 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1168 KREAEFQKMRRDLEEATL----QHEATAAALRKKHADSVAELG-------------EQIDNLQRVKQKLEKEKSELKMEI 1230
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGlapgrqsiidlkeKEIPELRNKLQKVNRDIQRLKNDI 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1231 DDLASNMETVSkAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQK---------ARLHTESGEFSRQLDEKEALVS 1301
Cdd:TIGR00606 768 EEQETLLGTIM-PEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdldrtvQQVNQEKQEKQHELDTVVSKIE 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1302 QLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHdcdlLREQYEEEQEAKAELQRGMSKANSEV---AQWRTKYE 1378
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ----FEEQLVELSTEVQSLIREIKDAKEQDsplETFLEKDQ 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1379 TDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKtkqRLQNEVEDLMIDVERSNAACIA----LDKKQRNFDKV 1454
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN---KIQDGKDDYLKQKETELNTVNAqleeCEKHQEKINED 999
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1455 LAEWKHKYEeTQAELEASQKESRSLSTELFKVKNAYEETL--------DQLETLKRENKNLQQEISDLTEQIAEGGKHIH 1526
Cdd:TIGR00606 1000 MRLMRQDID-TQKIQERWLQDNLTLRKRENELKEVEEELKqhlkemgqMQVLQMKQEHQKLEENIDLIKRNHVLALGRQK 1078
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1527 ELEKVKKQIDQEKSELQ-----ASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQS 1601
Cdd:TIGR00606 1079 GYEKEIKHFKKELREPQfrdaeEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQD 1158
|
810 820 830
....*....|....*....|....*....|
gi 826320982 1602 TLDAEIRSRNDALRIKKKMEGDLNEMEIQL 1631
Cdd:TIGR00606 1159 IEYIEIRSDADENVSASDKRRNYNYRVVML 1188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1380-1920 |
3.80e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1380 DAIHRTEELEEakKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLqneveDLMIDVERSNAACIALDKKQRnfdkvlaewK 1459
Cdd:COG4913 210 DDFVREYMLEE--PDTFEAADALVEHFDDLERAHEALEDAREQI-----ELLEPIRELAERYAAARERLA---------E 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1460 HKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGG--------KHIHELEKV 1531
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1532 KKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNH-------------LRVVES 1598
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALrdlrrelreleaeIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1599 MQSTLDAE---IRSR-NDALRIKkkmEGDL----NEMEIQLNHAN-RQASE-AIRNLRNTqgVLKDTQlHLDDAIRSQDD 1668
Cdd:COG4913 434 RKSNIPARllaLRDAlAEALGLD---EAELpfvgELIEVRPEEERwRGAIErVLGGFALT--LLVPPE-HYAAALRWVNR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1669 LKeqlamverranlmqaeveeLRASLeQTERSRKMAEQELLDASERVQLLHtqntslintkkKLETDISHIQGEMEDIVQ 1748
Cdd:COG4913 508 LH-------------------LRGRL-VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELG 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1749 E------ARNAEE--KAKKAITDAAMMAeelkkeQDTSAHlermkknmeqtVKDLQHRLDE--------AEQLALKggKK 1812
Cdd:COG4913 557 RrfdyvcVDSPEElrRHPRAITRAGQVK------GNGTRH-----------EKDDRRRIRSryvlgfdnRAKLAAL--EA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1813 QIQKLEARVRELENEVEgEQRRNVEAVKSLRKHERRVKELTY-------------QTEEDRKNVLRLQDLVDKLQTKVKA 1879
Cdd:COG4913 618 ELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWdeidvasaereiaELEAELERLDASSDDLAALEEQLEE 696
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 826320982 1880 YKRQAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVN 1920
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
889-1115 |
3.89e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 889 LQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEK 968
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 969 EKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAktkLEQQVDDLEGSLEQEKKLRM 1048
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA---RREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1049 DLERAKRKLEGDLKlaqestmDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQA 1115
Cdd:COG4942 168 ELEAERAELEALLA-------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1133-1735 |
4.02e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1133 KAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHE--------------------ATAA 1192
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKdlikennatrhlcnllketcARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1193 ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDlaSNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLI 1272
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAEN--ARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1273 NELSAQKAR------LHTESGEFSRQLDEKEALVS----QLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDC 1342
Cdd:pfam05483 247 IQITEKENKmkdltfLLEESRDKANQLEEKTKLQDenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1343 dllrEQYEEEQEAKAELQRGMSKANSEVAqwrTKYETDaihrTEELEEAKKKLAQRLQDAEEHVEAVN---SKCASLEKT 1419
Cdd:pfam05483 327 ----CQLTEEKEAQMEELNKAKAAHSFVV---TEFEAT----TCSLEELLRTEQQRLEKNEDQLKIITmelQKKSSELEE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1420 KQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLET 1499
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1500 LKR---------------------ENKNLQQEISDLTEQIAeggKHIHELEKVKKQIDQEKSELQaSLEEAEASLEHE-- 1556
Cdd:pfam05483 476 LKTelekeklknieltahcdklllENKELTQEASDMTLELK---KHQEDIINCKKQEERMLKQIE-NLEEKEMNLRDEle 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1557 -----------EGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEG--- 1622
Cdd:pfam05483 552 svreefiqkgdEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkql 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1623 -----DLNEMEIQLNHANRQASEAIRNLR-----------NTQGVLKDTQLHLDDAI--------RSQDDLKEQLAMVER 1678
Cdd:pfam05483 632 nayeiKVNKLELELASAKQKFEEIIDNYQkeiedkkiseeKLLEEVEKAKAIADEAVklqkeidkRCQHKIAEMVALMEK 711
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1679 RANLMQAEVEELRASLEQTErsRKMAEQELLDASERVQLLHTQNtSLINTKKKLETD 1735
Cdd:pfam05483 712 HKHQYDKIIEERDSELGLYK--NKEQEQSSAKAALEIELSNIKA-ELLSLKKQLEIE 765
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
869-1548 |
4.10e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 65.24 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 869 EAKRKELEEKMVTLMQEKNDLQLQVQAE-ADSLADAEERCDQLIKTKIQLEAKIKEATERAEdeEEINAELTAKKRKLED 947
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALE--SELREQLEAGKLEFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 948 ECSELKKDIDDLELTLAKVEKEKHATENK------VKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNT 1021
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1022 LTKAKTKLEQQVDDLEGSLEQekKLRMDLERAKRKLEGDLKLAQESTMDIEndkQQLDEKLKKKEFEMSNLQ---SKIED 1098
Cdd:pfam12128 518 RQSALDELELQLFPQAGTLLH--FLRKEAPDWEQSIGKVISPELLHRTDLD---PEVWDGSVGGELNLYGVKldlKRIDV 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1099 EQAVGMQlqkkiKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGAtsaqiemnkkreaeFQKMRR 1178
Cdd:pfam12128 593 PEWAASE-----EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA--------------LKNARL 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1179 DLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKgnFEKMCRTLEDQL 1258
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY--WQVVEGALDAQL 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1259 SEVKTKEEEQQrlinelSAQKARLHTESGEFSRQLDEK---EALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAV 1335
Cdd:pfam12128 732 ALLKAAIAARR------SGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETW 805
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1336 QSARhdcDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYET------DAIHRTEELEEAKKKLAQRLQDAEEHVEAv 1409
Cdd:pfam12128 806 LQRR---PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMerkaseKQQVRLSENLRGLRCEMSKLATLKEDANS- 881
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1410 nskcASLEKTKQRLQNEVEDLMIDVERsnaACIALDKKQRNFDKVLAewKHKYEETQAELEASQKESRSLSTELFKVKNa 1489
Cdd:pfam12128 882 ----EQAQGSIGERLAQLEDLKLKRDY---LSESVKKYVEHFKNVIA--DHSGSGLAETWESLREEDHYQNDKGIRLLD- 951
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 1490 YEETLDQLETLKreNKNLQQEISDLTEQIAEGGKHIHE----LEKVKKQIDQEKSELQASLEE 1548
Cdd:pfam12128 952 YRKLVPYLEQWF--DVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGE 1012
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
873-1274 |
5.14e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 873 KELEEKMVTLMQEK-----NDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKI----KEATERAEDEEEINAELTAKKR 943
Cdd:TIGR04523 291 NQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIsqlkKELTNSESENSEKQRELEEKQN 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 944 KLEDecseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLT 1023
Cdd:TIGR04523 371 EIEK----LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1024 KAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLklaqestmdiENDKQQLDEklKKKEFEMSNLQSKiedeqavg 1103
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL----------EQKQKELKS--KEKELKKLNEEKK-------- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1104 mQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEI-----SERLEEAGGATSAQIEMNKKREAEFQKMRR 1178
Cdd:TIGR04523 507 -ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1179 DLEEATLQHEATAAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQL 1258
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
410
....*....|....*.
gi 826320982 1259 SEVKTKEEEQQRLINE 1274
Cdd:TIGR04523 662 PEIIKKIKESKTKIDD 677
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
869-1211 |
5.19e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 869 EAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLiktkiqleAKIKEATERAEDEEEINAELTAKKRKLEde 948
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEIDVASAEREIAELEAELE-- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 949 csELKKDIDDLEltlaKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAktK 1028
Cdd:COG4913 679 --RLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--L 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1029 LEQQVDDLEGSlEQEKKLRMDLERAKRKLEGDLKLAQEstmDIENdkqQLDEKLKKKEFEMSNLQSKIEDE--------- 1099
Cdd:COG4913 751 LEERFAAALGD-AVERELRENLEERIDALRARLNRAEE---ELER---AMRAFNREWPAETADLDADLESLpeylalldr 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1100 -QAVGM-QLQKKIKELQarteeleeeieaERASRAKAEKQRSDLSRELEEISERLEEA---------GGATSAQIEMNKK 1168
Cdd:COG4913 824 lEEDGLpEYEERFKELL------------NENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPR 891
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 826320982 1169 REAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1211
Cdd:COG4913 892 PDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1064-1281 |
6.49e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1064 AQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSR 1143
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1144 ELEEISERLEE-------AGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELGEQIDNLQRVK 1216
Cdd:COG4942 98 ELEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 826320982 1217 QKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKAR 1281
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
869-1520 |
6.92e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 869 EAKRKELEEKMVTLMQEKNDLQLQVQAEADSLAD---AEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKL 945
Cdd:pfam05483 116 EAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnaTRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 946 EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAE-EDKVNTLTK 1024
Cdd:pfam05483 196 ILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEEsRDKANQLEE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1025 aKTKLeqQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVgm 1104
Cdd:pfam05483 276 -KTKL--QDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFV-- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1105 qlqkkIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatsaQIEMNKKREAEFQKMRRDL-EEA 1183
Cdd:pfam05483 351 -----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE-------MTKFKNNKEVELEELKKILaEDE 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1184 TLQHEataaalrKKHADSVAElgeqidNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKT 1263
Cdd:pfam05483 419 KLLDE-------KKQFEKIAE------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1264 KEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKrqlEEETKAKNALAHAVQSARHDCD 1343
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGD 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1344 LLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYET------DAIHRTEELEEAKKKLAQRLQDAEEHVEA----VNSKC 1413
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNlkkqieNKNKNIEELHQENKALKKKGSAENKQLNAyeikVNKLE 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1414 ASLEKTKQRL-------QNEVED-------LMIDVERSNAACIALDKKQRNFDK-----------VLAEWKHKY----EE 1464
Cdd:pfam05483 643 LELASAKQKFeeiidnyQKEIEDkkiseekLLEEVEKAKAIADEAVKLQKEIDKrcqhkiaemvaLMEKHKHQYdkiiEE 722
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 1465 TQAEL------EASQKESR-SLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAE 1520
Cdd:pfam05483 723 RDSELglyknkEQEQSSAKaALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1199-1415 |
9.33e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1199 ADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVktkEEEQQRLINELSAQ 1278
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1279 KARLHTESGEFSRQL---------DEKEALVS-----QLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDL 1344
Cdd:COG4942 96 RAELEAQKEELAELLralyrlgrqPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1345 LREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIhRTEELEEAKKKLAQRLQDAEEHVEAVNSKCAS 1415
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
865-1249 |
1.31e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEAD--SLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKK 942
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 943 RKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQE-------- 1003
Cdd:COG4717 177 EELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1004 ---AHQQTLDDLQAEEDKV---------------NTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQ 1065
Cdd:COG4717 257 allALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1066 ESTMDIENDKQQLDEKLKKKEfemsnlqskIEDEQAVGMQLQKKIKELQARTeelEEEIEAERASRAKAEKQRSDLSREL 1145
Cdd:COG4717 337 EELLELLDRIEELQELLREAE---------ELEEELQLEELEQEIAALLAEA---GVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1146 EEISERLEEAGGATSAQIEMNKKR--EAEFQKMRRDLEEATLQHEataaALRKKHADSVAELG--EQIDNLQRVKQKLEK 1221
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELE----ELREELAELEAELEqlEEDGELAELLQELEE 480
|
410 420 430
....*....|....*....|....*....|.
gi 826320982 1222 EKSELKMEIDDLASNM---ETVSKAKGNFEK 1249
Cdd:COG4717 481 LKAELRELAEEWAALKlalELLEEAREEYRE 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
884-1405 |
1.46e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 884 QEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATER-----AEDEEEINAELTAKKRKLED---ECSELKKD 955
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDRLEQLEREIERLERELEErerRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 956 IDDLELTLAKVEKE----KHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNT----LTKAKT 1027
Cdd:COG4913 368 LAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparLLALRD 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1028 KLEQQVDDLEGSL----------EQEKKLRMDLERA-----------------------KRKLEGDL-----KLAQESTM 1069
Cdd:COG4913 448 ALAEALGLDEAELpfvgelievrPEEERWRGAIERVlggfaltllvppehyaaalrwvnRLHLRGRLvyervRTGLPDPE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1070 DIENDKQQLDEKLKKKEFEMSN-LQSKIEDEQAV--------------GMQLQKKIKelQARTEELEEEIEAERASR--- 1131
Cdd:COG4913 528 RPRLDPDSLAGKLDFKPHPFRAwLEAELGRRFDYvcvdspeelrrhprAITRAGQVK--GNGTRHEKDDRRRIRSRYvlg 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1132 AKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAAALRKKHAD-SVAELGEQID 1210
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEA--------------EERLEALEAELDALQERREALQRLAEYSWDEiDVASAEREIA 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1211 NLQRVKQKLEKEKSELkmeiddlasnmetvskakgnfekmcRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFS 1290
Cdd:COG4913 672 ELEAELERLDASSDDL-------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1291 RQLDEKEALVSQLSRGKQAftQQIEELKRQLEEEtKAKNALAHAVQSARHDCDLLREQYEEEQEakaELQRGMSKANSE- 1369
Cdd:COG4913 727 EELDELQDRLEAAEDLARL--ELRALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEE---ELERAMRAFNREw 800
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 826320982 1370 ---VAQWRTKYET----DAIHR---TEELEEAKKKLAQRLQDAEEH 1405
Cdd:COG4913 801 paeTADLDADLESlpeyLALLDrleEDGLPEYEERFKELLNENSIE 846
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
938-1535 |
1.85e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.00 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 938 LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE---NIAKLAKEKKALQEAHQQTLDDLQA 1014
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1015 EEDKVNtltkaktkleqqvdDLEGSLEQEKKLRMDLERAKRklegdlklaqESTMDIENDKQQLDEKLKKkefeMSNLQS 1094
Cdd:PRK01156 268 ELEKNN--------------YYKELEERHMKIINDPVYKNR----------NYINDYFKYKNDIENKKQI----LSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1095 KIEDEQAVgmqlQKKIKELQArteeleeeieaERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQ 1174
Cdd:PRK01156 320 EINKYHAI----IKKLSVLQK-----------DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1175 KMRR---DLEEATLQHEATAAALRKKHadsvAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKakgnfEKMC 1251
Cdd:PRK01156 385 NIERmsaFISEILKIQEIDPDAIKKEL----NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNG-----QSVC 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1252 RTLEDQLSevktkEEEQQRLINELSAQKARLHTESGEFSRQ---LDEK--------EALVSQLSRGKQAFTQQIEELKRQ 1320
Cdd:PRK01156 456 PVCGTTLG-----EEKSNHIINHYNEKKSRLEEKIREIEIEvkdIDEKivdlkkrkEYLESEEINKSINEYNKIESARAD 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1321 LEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAElqrGMSKANSEvaqwRTKYETDAIH-RTEELEEAKKKLAQRL 1399
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRT---SWLNALAV----ISLIDIETNRsRSNEIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1400 QDAEEHVEAVNSkcaSLEKTKQRLQNEVEDL---MIDVERSNAACIALDKKQRNFDKVLAEwKHKYEETQAELEASQKES 1476
Cdd:PRK01156 604 QEIEIGFPDDKS---YIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDI 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1477 rslSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQI 1535
Cdd:PRK01156 680 ---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
916-1244 |
2.89e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.83 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 916 QLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLA 995
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 996 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDK 1075
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1076 QQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSR------------ 1143
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1144 -----ELEEISERLEEA------GGATSAQ--------IEMNKKR----EAEFQKMRRDLEEATLQHEATAAAL------ 1194
Cdd:pfam07888 275 hqarlQAAQLTLQLADAslalreGRARWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELgrekdc 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1195 -RKKHADSVAELGEQIDNL---QRVKQKLEKEKSELKMEIDDLASNMETVSKAK 1244
Cdd:pfam07888 355 nRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1313-1842 |
4.22e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1313 QIEELKRQLEE-ETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAElQRGmsKANSEVAQWRTKYEtdaihRTEELEEA 1391
Cdd:PRK02224 188 SLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARE-TRD--EADEVLEEHEERRE-----ELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1392 KKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEE------- 1464
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaaqa 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1465 --TQAE--------LEASQKESRS----LSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEK 1530
Cdd:PRK02224 340 hnEEAEslredaddLEERAEELREeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1531 VKKQIDQEKSELQASLEEAEASLEH-----EEGK------------------------------ILRIQLELNQVKSEID 1575
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEaeallEAGKcpecgqpvegsphvetieedrerveeleaeLEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1576 R--KIAEKDEEIDQLkRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLN-EMEIQLNHANRQASEAiRNLRNTQGVL 1652
Cdd:PRK02224 500 RaeDLVEAEDRIERL-EERREDLEELIAERRETIEEKRERAEELRERAAELEaEAEEKREAAAEAEEEA-EEAREEVAEL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1653 KDTQLHLDDAIRSQDDLKEQLAMVERranlMQAEVEELRASLEQ-TERSRKMAEQeLLDASERvqllhtqntslintKKK 1731
Cdd:PRK02224 578 NSKLAELKERIESLERIRTLLAAIAD----AEDEIERLREKREAlAELNDERRER-LAEKRER--------------KRE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1732 LETDIShiqgemEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLD--EAEQLALKG 1809
Cdd:PRK02224 639 LEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREalENRVEALEA 712
|
570 580 590
....*....|....*....|....*....|...
gi 826320982 1810 GKKQIQKLEARVRELENEVegeQRRNVEAVKSL 1842
Cdd:PRK02224 713 LYDEAEELESMYGDLRAEL---RQRNVETLERM 742
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1445-1933 |
4.51e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1445 DKKQRNFDKVLAEWKHKYEETQAELE--ASQKE-SRSLSTELFKVKNAYEETLDQLETLKrenknlqQEISDLTEQIAEG 1521
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIEryEEQREqARETRDEADEVLEEHEERREELETLE-------AEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1522 GKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQL---ELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVES 1598
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEArreELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1599 MqstldAEIRSRNDALRIK-KKMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAirsqDDLKEQLAmvE 1677
Cdd:PRK02224 351 A-----DDLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA----EDFLEELR--E 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1678 RRANLMQaEVEELRASLeQTERSRKMAEQELLDAS---ERVQLLhtQNTSLINTKKKLETDISHIQGEMEDIVQEARNAE 1754
Cdd:PRK02224 420 ERDELRE-REAELEATL-RTARERVEEAEALLEAGkcpECGQPV--EGSPHVETIEEDRERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1755 EKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELENEVEGEQRR 1834
Cdd:PRK02224 496 ERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRE--------RAEELRERAAELEAEAEEKREA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1835 NVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDkLQTKVKAYKRQAEEAEEQ------------------------ 1890
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT-LLAAIADAEDEIERLREKrealaelnderrerlaekrerkre 638
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 826320982 1891 --SNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1933
Cdd:PRK02224 639 leAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1107-1339 |
4.94e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1107 QKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEeaggATSAQIemnKKREAEFQKMRRDLEEATLQ 1186
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA----ALARRI---RALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1187 heatAAALRKKHADSVAELGEQIDNLQRVKQKlekekSELKM-----EIDDLASNMETVSKAKGNFEKMCRTLEDQLSEV 1261
Cdd:COG4942 92 ----IAELRAELEAQKEELAELLRALYRLGRQ-----PPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1262 KTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSAR 1339
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
844-1318 |
5.22e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.28 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 844 SAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKE 923
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 924 -ATERAEDE---------EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAG------- 986
Cdd:pfam05483 410 lKKILAEDEklldekkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknie 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 987 LDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEgslEQEKKLRMDLERAKRKL--EGD---- 1060
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFiqKGDevkc 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1061 -LKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQavgmqlqKKIKELQARTEELEEEIEAERASRAKAEKQRS 1139
Cdd:pfam05483 567 kLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-------KNIEELHQENKALKKKGSAENKQLNAYEIKVN 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1140 DLSRELEEISERLEEAGGATSAQIEMNKKREaefQKMRRDLEEAtlqheataaalrKKHADSVAELGEQIDnlQRVKQKl 1219
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNYQKEIEDKKISE---EKLLEEVEKA------------KAIADEAVKLQKEID--KRCQHK- 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1220 ekekselkmeIDDLASNMEtvsKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEAL 1299
Cdd:pfam05483 702 ----------IAEMVALME---KHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
490
....*....|....*....
gi 826320982 1300 VSQLSRGKQAFTQQIEELK 1318
Cdd:pfam05483 769 KEKLKMEAKENTAILKDKK 787
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1315-1710 |
5.25e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.06 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1315 EELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVaqwrtkyETDAIHRTEELEEAKKK 1394
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAEL-------KEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1395 LAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEE---TQAELEA 1471
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1472 SQKESRSLSTELFKVKNAYEETLDQLETlkrenknLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEA 1551
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1552 sleheegkilriqlelnqVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQL 1631
Cdd:pfam07888 256 ------------------LGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1632 NHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERranlmqaEVEELRASLE--QTERSRKMAE-QEL 1708
Cdd:pfam07888 318 DRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRR-------ELQELKASLRvaQKEKEQLQAEkQEL 390
|
..
gi 826320982 1709 LD 1710
Cdd:pfam07888 391 LE 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
931-1361 |
6.59e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 931 EEEINAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKAL--QEAHQQT 1008
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1009 LDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlKLAQESTMDIENDKQQLDEKLKKKEFE 1088
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1089 MSNLQSKIEdeqavgmQLQKKIKELQARTEELEEEIEAERASRAKAEKQRS--------DLSRELEEISERLEEAGGAT- 1159
Cdd:COG4717 208 LAELEEELE-------EAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1160 ---------------SAQIEMNKKREAEFQKMRRDLEEATLQheATAAALRKKHADSVAELGEQIDNLQRVKQKL-EKEK 1223
Cdd:COG4717 281 lvlgllallflllarEKASLGKEAEELQALPALEELEEEELE--ELLAALGLPPDLSPEELLELLDRIEELQELLrEAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1224 SELKMEIDDLASNMETVSKAKGNfekmcrTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLD--EKEALVS 1301
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGV------EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1302 QLSRgkqaFTQQIEELKRQLEEETKAKNALAHAVQSARHDcDLLREQYEEEQEAKAELQR 1361
Cdd:COG4717 433 ELEE----LEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRE 487
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
833-1506 |
7.41e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.22 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 833 KLYFKIKPLLKSAETEKEMANMKEEFEKAKEELAKSE--AKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAE------ 904
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 905 ERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 977
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 978 KNLTEEMAGLDENIAKLAKekkalQEAHQQTLDDLQAEEDKVNT----LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERA 1053
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1054 KRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAK 1133
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1134 AEKQRSDLSRELEEISERLEEAGGATSAQIEMnKKREAEFQKMRRDLEEATLqhEATAAALRKKHADSVAEL---GEQID 1210
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELdtvVSKIE 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1211 NLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVktkeeeqQRLINELSAQKARLHTESGEFS 1290
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-------QSLIREIKDAKEQDSPLETFLE 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1291 RQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAK-AELQRGMSKANSE 1369
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINED 999
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1370 VAQWRTKYETDAIH------------RTEELEEAKKKLAQRLQDAEEhveavnSKCASLEKTKQRLQNEVEDLMIDVERS 1437
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQEHQKLEENIDLIKRNHVLA 1073
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1438 NAACIALDKKQRNFDKVLAEWKHK-YEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKN 1506
Cdd:TIGR00606 1074 LGRQKGYEKEIKHFKKELREPQFRdAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1003-1493 |
7.49e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1003 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQESTMDIENDKQQLdEKL 1082
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERL-EEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1083 KKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRA-KAEKQRSDLSRELEEISERLEEAggatSA 1161
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELeELQQRLAELEEELEEAQEELEEL----EE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1162 QIEmNKKREAEFQKMRRDLEEATLQHEATAAALrkkhadSVAELGEQIDNLQRVKQKLekekseLKMEIDDLASNMETVS 1241
Cdd:COG4717 228 ELE-QLENELEAAALEERLKEARLLLLIAAALL------ALLGLGGSLLSLILTIAGV------LFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1242 KAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRG-KQAFTQQIEELKRQ 1320
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1321 LEEETKAKN--ALAHAVQSArhdcdllrEQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAihrteeleeakkkLAQR 1398
Cdd:COG4717 375 LLAEAGVEDeeELRAALEQA--------EEYQELKEELEELEEQLEELLGELEELLEALDEEE-------------LEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1399 LQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVErsnaacialdkkqrnfdkvLAEWKHKYEETQAELEASQKESRS 1478
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEEDGE-------------------LAELLQELEELKAELRELAEEWAA 494
|
490
....*....|....*
gi 826320982 1479 LSTELFKVKNAYEET 1493
Cdd:COG4717 495 LKLALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1495-1718 |
9.23e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1495 DQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEI 1574
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1575 DRKIAEKDEEIDQLKRNhlrvveSMQSTLDAEIRSRNDAlrikkkmegDLNEMEIQLNHANRQASEAIRNLRNTQGVLKD 1654
Cdd:COG4942 100 EAQKEELAELLRALYRL------GRQPPLALLLSPEDFL---------DAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1655 TQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLL 1718
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
865-1353 |
1.09e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQlQVQAEADSLADAEERCDQliktKIQLEAKIKEATERAEDEEEINAELTAKKRK 944
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELRE----ELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 945 LEdecsELKKDIDDLEltlakvekekhATENKVKNLTEEMAGLDENIAKLAKEKKALQEAH-QQTLDDLQAEEDKVNTLT 1023
Cdd:COG4717 148 LE----ELEERLEELR-----------ELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1024 KAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIendKQQLDEKLKKKEFEMSNLQSKIEDEQAVG 1103
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA---LLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1104 MQ-LQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEE 1182
Cdd:COG4717 290 FLlLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1183 ATLQheataAALRKKHADSVAELGEQIDNLQRvKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEkmcrtLEDQLSEVK 1262
Cdd:COG4717 370 QEIA-----ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1263 TKEEEQQRLINELSAQKARLHTEsgefSRQLDEKEALVSQLsrgkqaftQQIEELKRQLEEETKAKNALAHAVQSARHdc 1342
Cdd:COG4717 439 EELEELEEELEELREELAELEAE----LEQLEEDGELAELL--------QELEELKAELRELAEEWAALKLALELLEE-- 504
|
490
....*....|.
gi 826320982 1343 dlLREQYEEEQ 1353
Cdd:COG4717 505 --AREEYREER 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1670-1933 |
1.20e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1670 KEQLAMVERRANLMQAEVEELRASLEQTERSRKMAE--QELLDASERVQLlhtqnTSLINTKKKLETDISHIQGEMEDIV 1747
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEG-----YELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1748 QEARNAEEKAkkaitdaammaEELKKEqdtSAHLERMKKNMEQTVKDLqhrlDEAEQLALKGG----KKQIQKLEARVRE 1823
Cdd:TIGR02169 251 EELEKLTEEI-----------SELEKR---LEEIEQLLEELNKKIKDL----GEEEQLRVKEKigelEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1824 LENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLARFRKIQH 1903
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270
....*....|....*....|....*....|
gi 826320982 1904 ELEEAEERADIAESQVNKLRVKSREVHTKI 1933
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEEL 422
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1164-1893 |
1.30e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 60.45 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1164 EMNKKREAEFQKMRrDLEEATLQ-HEATAAALRKKHADSVAEL-----GEQIDNLQRVKQKLEKEKSELKMEIDDLASNM 1237
Cdd:TIGR01612 700 DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGEINKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1238 ETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQrlinelsaqkaRLHTESGEFSRQLDEKEALVSQLsrgkqaftqqIEEL 1317
Cdd:TIGR01612 779 DELNKYKSKISEIKNHYNDQINIDNIKDEDAK-----------QNYDKSKEYIKTISIKEDEIFKI----------INEM 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1318 KRQLEEETKAKNALAHAVQSARHDCDLLREQYEE-EQEAKAELqrgmskANSEVAQWRTKYETDA--IHRTEELEEAKKK 1394
Cdd:TIGR01612 838 KFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAElTNKIKAEI------SDDKLNDYEKKFNDSKslINEINKSIEEEYQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1395 LAQRLQDAEEHVEAVNSKCASLEK--TKQRLQNEVEDLMIDVERSNAaciALDKKQRN-FDKVLAEWKHKYEETQAELEA 1471
Cdd:TIGR01612 912 NINTLKKVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTIKESN---LIEKSYKDkFDNTLIDKINELDKAFKDASL 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1472 SQKESRslSTELFKVKNAYEETL---------DQLETLKRENKNLQQEISDLTEQIAEGGKHIHE-----LEKVKKQIDQ 1537
Cdd:TIGR01612 989 NDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTsiyniIDEIEKEIGK 1066
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1538 EKSELQAS-LEEAEASLEHEEGkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNhlrvVESMQSTLDAEIrsrNDALRI 1616
Cdd:TIGR01612 1067 NIELLNKEiLEEAEINITNFNE--IKEKLKHYNFDDFGKEENIKYADEINKIKDD----IKNLDQKIDHHI---KALEEI 1137
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1617 KKKMEGDLNEMEIQLNHANRQASEAIRNlRNTQGVLKDTQ---LHLDDAIRSQDDLKE---QLAMVERRANLMQaEVEEL 1690
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKIEnivTKIDKKKNIYDEIKKllnEIAEIEKDKTSLE-EVKGI 1215
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1691 RAS---------LEQTERSRKMAE----------QELLDASERVQLLHTQNTSLINTKKKLET-DISHIQGEMEDIVQEA 1750
Cdd:TIGR01612 1216 NLSygknlgklfLEKIDEEKKKSEhmikameayiEDLDEIKEKSPEIENEMGIEMDIKAEMETfNISHDDDKDHHIISKK 1295
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1751 RNaeekakKAITDaaMMAEELKKEQDTSAhlermKKNMEQTVKDLQHRLDEAeqlalkggkkqiQKLEARVRELENEVeg 1830
Cdd:TIGR01612 1296 HD------ENISD--IREKSLKIIEDFSE-----ESDINDIKKELQKNLLDA------------QKHNSDINLYLNEI-- 1348
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 1831 EQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVlrlQDLVDKLQTKVKAYKRQAEEAEEQSNV 1893
Cdd:TIGR01612 1349 ANIYNILKLNKIKKIIDEVKEYTKEIEENNKNI---KDELDKSEKLIKKIKDDINLEECKSKI 1408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1463-1680 |
1.93e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1463 EETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSEL 1542
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1543 QASLEEAEASLeHEEGKILRIQLELNQVKSEidrKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEG 1622
Cdd:COG4942 103 KEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1623 DLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRA 1680
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1228-1701 |
2.12e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1228 MEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGK 1307
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1308 QAFT--QQIEELKRQLEEETKAKNALAHAVQSARHdcdlLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRT 1385
Cdd:COG4717 126 QLLPlyQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1386 EELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQ--NEVEDLMIDVERSNAACIALDKKQRNFDKV--------- 1454
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1455 ---LAEWKHKYEETQAELEASQKESRSLSTELFKVKNayEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKV 1531
Cdd:COG4717 282 vlgLLALLFLLLAREKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1532 KKQIDQE--KSELQASLEEAEASLEHEegkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQ-STLDAEIR 1608
Cdd:COG4717 360 EEELQLEelEQEIAALLAEAGVEDEEE----LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1609 SRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRnlrntqgvlkdtqlhLDDAIRSQDDLKEQLAMVERRANLMQAEVE 1688
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGE---------------LAELLQELEELKAELRELAEEWAALKLALE 500
|
490
....*....|...
gi 826320982 1689 ELRASLEQTERSR 1701
Cdd:COG4717 501 LLEEAREEYREER 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1129-1332 |
2.78e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1129 ASRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQ 1208
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1209 IDNLQrvkQKLEKEKSELKM----------------------EIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEE 1266
Cdd:COG3883 74 IAEAE---AEIEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 1267 EQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALA 1332
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
865-1702 |
2.93e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKiQLEAKIKEATERAEDEEEINAELTAKKRK 944
Cdd:PRK04863 302 LAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERLEEQNEVVEEADEQQEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 945 LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEniaklAKEKKALQEAHQQTLDDLQAE-EDKVNTLT 1023
Cdd:PRK04863 381 NEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALER-----AKQLCGLPDLTADNAEDWLEEfQAKEQEAT 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1024 KAKTKLEQQVDDLEGSLEQ-EKKLR--------MDLERAKRKlegdlklAQESTMDIENDKQQlDEKLKKKEFEMSNLQS 1094
Cdd:PRK04863 456 EELLSLEQKLSVAQAAHSQfEQAYQlvrkiageVSRSEAWDV-------ARELLRRLREQRHL-AEQLQQLRMRLSELEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1095 KIEDEQAV-------GMQLQKKI---KELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEIserleeaggatSAQIE 1164
Cdd:PRK04863 528 RLRQQQRAerllaefCKRLGKNLddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL-----------QARIQ 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1165 MNKKREAEFqkmrrdleeatLQHEATAAALRKKHADSVA---ELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVS 1241
Cdd:PRK04863 597 RLAARAPAW-----------LAAQDALARLREQSGEEFEdsqDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1242 KAKGNFEKMCRTLEDQLSEVKTKE-------EE------------QQRLINELSAQKARLHTE----------------- 1285
Cdd:PRK04863 666 QPGGSEDPRLNALAERFGGVLLSEiyddvslEDapyfsalygparHAIVVPDLSDAAEQLAGLedcpedlyliegdpdsf 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1286 -SGEFSRQLDEKEALV------SQLSR-------GKQAFTQQIEELKRQLEEETKAKNALAHAVQsarhDCDLLREQYE- 1350
Cdd:PRK04863 746 dDSVFSVEELEKAVVVkiadrqWRYSRfpevplfGRAAREKRIEQLRAEREELAERYATLSFDVQ----KLQRLHQAFSr 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1351 ------------EEQEAKAELQRGMSKANSEVAQwrtkyetdaihrteeLEEAKKKLAQRLQDAEEHVEAVNsKCASLEK 1418
Cdd:PRK04863 822 figshlavafeaDPEAELRQLNRRRVELERALAD---------------HESQEQQQRSQLEQAKEGLSALN-RLLPRLN 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1419 TKQR--LQNEVEDLMIDVERSNAACIALDKKQRNFDKV-------------LAEWKHKYEETQAELEASQKESRSLsTEL 1483
Cdd:PRK04863 886 LLADetLADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqFEQLKQDYQQAQQTQRDAKQQAFAL-TEV 964
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1484 FKVKN--AYEETLDQL-------ETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLE 1554
Cdd:PRK04863 965 VQRRAhfSYEDAAEMLaknsdlnEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQ 1044
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1555 heegkilriQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRV--VESMQSTLDAEIRSRNDALRikkKMEGDLNEMEIQLN 1632
Cdd:PRK04863 1045 ---------DLGVPADSGAEERARARRDELHARLSANRSRRnqLEKQLTFCEAEMDNLTKKLR---KLERDYHEMREQVV 1112
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1633 HANRQASEAIRNLRNTqGVLKdtQLHL-DDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRK 1702
Cdd:PRK04863 1113 NAKAGWCAVLRLVKDN-GVER--RLHRrELAYLSADELRSMSDKALGALRLAVADNEHLRDVLRLSEDPKR 1180
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
982-1924 |
3.03e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 982 EEMAGLDENIAKLAKEK---KALQEAHQQTLDDLQAEEDkvnTLTKAKTKLEQQVDDLEGSL----------EQEKKLRM 1048
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1049 DLERAKRKLEGDL---KLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQarteeleeeie 1125
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1126 aerasRAKAEKQRSDLsrELEEISERLEEAggATSAQIEMNKKREAEfQKMRrDLEEATLQHEATAAALRKkhadsvaeL 1205
Cdd:PRK04863 425 -----RAKQLCGLPDL--TADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------I 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1206 GEQID--NLQRVKQKLEKEKSELKMEIDDLASnmetvskakgnfekmcrtLEDQLSEVKTKEEEQQ---RLINELSAQKA 1280
Cdd:PRK04863 486 AGEVSrsEAWDVARELLRRLREQRHLAEQLQQ------------------LRMRLSELEQRLRQQQraeRLLAEFCKRLG 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1281 RLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEE---ETKAKNALAHAVQSARHDCDLLREQYEEEQE--- 1354
Cdd:PRK04863 548 KNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqaRIQRLAARAPAWLAAQDALARLREQSGEEFEdsq 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1355 -------AKAELQRGMSKANSEVAQwrtkyetdaihRTEELEEAKKKLAQ-------RLQDAEEHVEAV----------- 1409
Cdd:PRK04863 628 dvteymqQLLERERELTVERDELAA-----------RKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsl 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1410 -----------NSKCA----SLEKTKQRLQNEvEDLMIDVERSNAACIALDkkqrnfDKVLAEWKHKYEETQAELEASQK 1474
Cdd:PRK04863 697 edapyfsalygPARHAivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFD------DSVFSVEELEKAVVVKIADRQWR 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1475 ESRSLSTELFKvKNAYEETLDQLetlkrenknlQQEISDLTEQIAEGGKHIHELEKVKKQIDQ----------------E 1538
Cdd:PRK04863 770 YSRFPEVPLFG-RAAREKRIEQL----------RAEREELAERYATLSFDVQKLQRLHQAFSRfigshlavafeadpeaE 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1539 KSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID--RKIAEkdeEIDQLKRNHL--RVVEsmqstLDAEIRSRNDAL 1614
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSalNRLLP---RLNLLADETLadRVEE-----IREQLDEAEEAK 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1615 RIKKKMEGDLNEMEIQLNhANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLkeqlamVERRANLMQAE-------- 1686
Cdd:PRK04863 911 RFVQQHGNALAQLEPIVS-VLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEV------VQRRAHFSYEDaaemlakn 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1687 ---VEELRASLEQTERSRKMAEQELLDASERvqllHTQN----TSLINTKKKLETDISHIQGEMEDI-VQEARNAEEKak 1758
Cdd:PRK04863 984 sdlNEKLRQRLEQAEQERTRAREQLRQAQAQ----LAQYnqvlASLKSSYDAKRQMLQELKQELQDLgVPADSGAEER-- 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1759 kaitdAAMMAEELKKEQDTSahleRMKKN-MEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELENEVEGEQRRNVE 1837
Cdd:PRK04863 1058 -----ARARRDELHARLSAN----RSRRNqLEKQLTFCEAEMDNLT--------KKLRKLERDYHEMREQVVNAKAGWCA 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1838 AVKSLRKH--ERRV--KELTYQT---------------------EEDRKNVLRLQDLVDKLQTKVKAY-------KRQAE 1885
Cdd:PRK04863 1121 VLRLVKDNgvERRLhrRELAYLSadelrsmsdkalgalrlavadNEHLRDVLRLSEDPKRPERKVQFYiavyqhlRERIR 1200
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 826320982 1886 ----------EAEEQSNVNLARfrkIQHELEEAEERADIA-ESQVNKLRV 1924
Cdd:PRK04863 1201 qdiirtddpvEAIEQMEIELSR---LTEELTSREQKLAISsESVANIIRK 1247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
971-1196 |
3.51e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 971 HATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSL----EQEKKL 1046
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1047 RMDLERAKRKLEGDL----KLAQESTMDI---ENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEE 1119
Cdd:COG4942 96 RAELEAQKEELAELLralyRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1120 LEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRK 1196
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1497-1931 |
3.93e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 58.68 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1497 LETL--KRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLE-EAEASLEHEEGKILRIQLELNQVK-S 1572
Cdd:pfam10174 164 LEMLqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1573 EIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMeiqlnhaNRQASEairnLRNTQGVL 1652
Cdd:pfam10174 244 SLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQEL-------SKKESE----LLALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1653 KDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKL 1732
Cdd:pfam10174 313 ETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVK 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1733 ETDISHIQGEMEDIVQEARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQTVKDLQHRLDEAEQ 1804
Cdd:pfam10174 393 ERKINVLQKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELES 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1805 L--ALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQtkvkaykr 1882
Cdd:pfam10174 473 LkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH-------- 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 826320982 1883 QAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHT 1931
Cdd:pfam10174 545 NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1076-1543 |
4.49e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1076 QQLDEKLKKKEFEMSNLQSKIEDEQAVGMQ---LQKKIKELQA--RTEELEEEIEAERASRAKAEKQRSDLSRELEEISE 1150
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEEleeLEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1151 RLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEI 1230
Cdd:COG4717 154 RLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1231 DDLASNMETVSKAKgnfekmcrtledqlsevktKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEAL----------V 1300
Cdd:COG4717 230 EQLENELEAAALEE-------------------RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1301 SQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWrtkyetd 1380
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL------- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1381 aihRTEELEEAKKKLAQRLQDAEEhvEAVNSKCASLEKtKQRLQNEVEDLMIDVERSNAACIALDKKQrnfdkVLAEWKH 1460
Cdd:COG4717 364 ---QLEELEQEIAALLAEAGVEDE--EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEAL-----DEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1461 KYEETQAELEASQKESRSLSTELFKVKNayeetldQLETLKRENK--NLQQEISDLTEQIAEGGKHIHELEKVKKQIDQE 1538
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEA-------ELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEA 505
|
....*
gi 826320982 1539 KSELQ 1543
Cdd:COG4717 506 REEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1347-1584 |
4.57e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1347 EQYEEEQEAKAELQRGMSKANSEVAQWRTKyETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNE 1426
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1427 vedlmidversnaaciaLDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKN 1506
Cdd:COG4942 99 -----------------LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1507 LQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEE 1584
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1390-1617 |
4.73e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1390 EAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAEL 1469
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1470 E-----------ASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKkqidQE 1538
Cdd:COG4942 100 EaqkeelaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER----AE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1539 KSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIK 1617
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1271-1711 |
4.76e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1271 LINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLR---- 1346
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1347 --EQYEEEQEAKAELQRGMSKANS---EVAQWRTKyETDAIHRTEELEEAKKKLA-----------QRLQDAEEHVEAVN 1410
Cdd:COG4717 127 llPLYQELEALEAELAELPERLEEleeRLEELREL-EEELEELEAELAELQEELEelleqlslateEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1411 SKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDK-----------VLAEWKHKYEETQAELEASQKESRSL 1479
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1480 ----STELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQI-AEGGKHIHELEKVKKQIDQEKsELQASLEEAEASLE 1554
Cdd:COG4717 286 lallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALgLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1555 HEEGKILRIQL-ELNQVKSEID-RKIAEKDEEIDQLKRNhlrvVESMQSTLDAEIRSRNDALRikkkmEGDLNEMEIQLN 1632
Cdd:COG4717 365 LEELEQEIAALlAEAGVEDEEElRAALEQAEEYQELKEE----LEELEEQLEELLGELEELLE-----ALDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1633 HANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQ--DDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLD 1710
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
.
gi 826320982 1711 A 1711
Cdd:COG4717 516 P 516
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1196-1773 |
7.05e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1196 KKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDdlasnmeTVSKAKGNFEKMCRTLEDQLSEVKTKEEEqqrlINEL 1275
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYN-------NAMDDYNNLKSALNELSSLEDMKNRYESE----IKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1276 SAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSaRHDCDLLREQYEEEQEA 1355
Cdd:PRK01156 262 ESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK-YHAIIKKLSVLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1356 KAELQRGMSKANSEVAQWRTkYETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVE 1435
Cdd:PRK01156 341 YIKKKSRYDDLNNQILELEG-YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1436 RSNAACIALDKKQRNfdkvLAEWKHKYEETQAELEASQKE---SRSLSTE-LFKVKNAYEETLDQLETLKREnknLQQEI 1511
Cdd:PRK01156 420 DISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQSVCpvcGTTLGEEkSNHIINHYNEKKSRLEEKIRE---IEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1512 SDLTEQIAEGGKHIHELEKvkKQIDQEKSELQaSLEEAEASLEHEEGKILRIQlELNQVKSEIDRKIAEKDEEIDQLKRN 1591
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLES--EEINKSINEYN-KIESARADLEDIKIKINELK-DKHDKYEEIKNRYKSLKLEDLDSKRT 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1592 HLRVVESMQSTLDAE-IRSRNDALRIK-KKMEGDLNEMEIQLNHAN-------RQASEAIRNLRNTQGVLKDTQLHLDDA 1662
Cdd:PRK01156 569 SWLNALAVISLIDIEtNRSRSNEIKKQlNDLESRLQEIEIGFPDDKsyidksiREIENEANNLNNKYNEIQENKILIEKL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1663 IRSQDDLKEQLAMVERRanlmQAEVEELRASLEQTERSRKMAEQELLDAservqllhtqNTSLINTKKKLETDISHIQgE 1742
Cdd:PRK01156 649 RGKIDNYKKQIAEIDSI----IPDLKEITSRINDIEDNLKKSRKALDDA----------KANRARLESTIEILRTRIN-E 713
|
570 580 590
....*....|....*....|....*....|....
gi 826320982 1743 MEDIVQEARNAEEKAKK---AITDAAMMAEELKK 1773
Cdd:PRK01156 714 LSDRINDINETLESMKKikkAIGDLKRLREAFDK 747
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
865-1702 |
8.00e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.65 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEkndLQLQVQAEADSLADAEERCD--QLIKTKIQLEAKI-------KEATERAEDEEEIN 935
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARE---LEELSARESDLEQDYQAASDhlNLVQTALRQQEKIeryqedlEELTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 936 AELTAKkrkledecselkkdiddleltLAKVEKEKHATENKVKNLTEEMA----GLDENIAKLAKEKKALQ---EAHQQT 1008
Cdd:COG3096 371 EEAAEQ---------------------LAEAEARLEAAEEEVDSLKSQLAdyqqALDVQQTRAIQYQQAVQaleKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1009 -LDDLqAEEDKVNTLTKAKTKLEQQVDDLegsLEQEKKLRMDlERAKRKLEGDLKLAQesTMDIENDKQQLDEKLKKKEF 1087
Cdd:COG3096 430 gLPDL-TPENAEDYLAAFRAKEQQATEEV---LELEQKLSVA-DAARRQFEKAYELVC--KIAGEVERSQAWQTARELLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1088 EMSNLQSKIEDEQAVGMQLqkkiKELQARTeeleeeieaerASRAKAEKQRSDLSR----------ELEEISERLEeagg 1157
Cdd:COG3096 503 RYRSQQALAQRLQQLRAQL----AELEQRL-----------RQQQNAERLLEEFCQrigqqldaaeELEELLAELE---- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1158 atsAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKK-----HADSVAE-----LGEQIDNLQRV----KQKLEKEK 1223
Cdd:COG3096 564 ---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALErlreqSGEALADSQEVtaamQQLLERER 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1224 sELKMEIDDLA-------SNMETVSKAKGNFEKMCRTLEDQLSEVKTKE-------------------EEQQRLINELSA 1277
Cdd:COG3096 641 -EATVERDELAarkqaleSQIERLSQPGGAEDPRLLALAERLGGVLLSEiyddvtledapyfsalygpARHAIVVPDLSA 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1278 QKARLHTES----------------GEFSRQLDEKE-ALVSQLSR--------------GKQAFTQQIEELKRQLEEETK 1326
Cdd:COG3096 720 VKEQLAGLEdcpedlyliegdpdsfDDSVFDAEELEdAVVVKLSDrqwrysrfpevplfGRAAREKRLEELRAERDELAE 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1327 AKNALAHAVQS------------ARHDCDLLREQYEEE----QEAKAELQRGMSKANSEVAQWRTKYETDA--------- 1381
Cdd:COG3096 800 QYAKASFDVQKlqrlhqafsqfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQQLDQLKeqlqllnkl 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1382 IHRTEELEEAkkKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQnEVEDlMIDVERSNAAcialdkkqrnfdkvlaewkhK 1461
Cdd:COG3096 880 LPQANLLADE--TLADRLEELREELDAAQEAQAFIQQHGKALA-QLEP-LVAVLQSDPE--------------------Q 935
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1462 YEETQAELEASQKESRSLSTELFKVKN--------AYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKK 1533
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEvvqrrphfSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYS 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1534 QIDQEKSELQASLEEAEASLEHEEGKILriQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRV--VESMQSTLDAEIRSRN 1611
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELE--ELGVQADAEAEERARIRRDELHEELSQNRSRRsqLEKQLTRCEAEMDSLQ 1093
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1612 DALRikkKMEGDLNEMEIQLNHAnrQAS-EAIRNLRNTQGVLKdtQLHLDD-AIRSQDDLKEQLAMVERRANLMQAEVEE 1689
Cdd:COG3096 1094 KRLR---KAERDYKQEREQVVQA--KAGwCAVLRLARDNDVER--RLHRRElAYLSADELRSMSDKALGALRLAVADNEH 1166
|
970
....*....|...
gi 826320982 1690 LRASLEQTERSRK 1702
Cdd:COG3096 1167 LRDALRLSEDPRR 1179
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1452-1619 |
8.04e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.32 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1452 DKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKH------I 1525
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1526 HELEKVKKQIDQ---EKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNhlrvVESMQST 1602
Cdd:COG1579 96 KEIESLKRRISDledEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REELAAK 171
|
170
....*....|....*..
gi 826320982 1603 LDAEIRSRNDALRIKKK 1619
Cdd:COG1579 172 IPPELLALYERIRKRKN 188
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1268-1937 |
9.13e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.67 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1268 QQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKnalahavQSARHDCDLLRE 1347
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-------KLKEQAKKALEY 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1348 QYEEEQEAKAELQRGMSKANSEVAQWRTKYETDaihrtEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEV 1427
Cdd:pfam02463 213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL-----LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1428 EDLMIDVERSNAACIALDKKQRNFD-KVLAEWKHKYEETQAELEASQKESRSLSTEL-FKVKNAYEETLDQLETLKRENK 1505
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDeEKLKESEKEKKKAEKELKKEKEEIEELEKELkELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1506 NLQQEISDLTEQiaegGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQ--VKSEIDRKIAEKDE 1583
Cdd:pfam02463 368 LEQLEEELLAKK----KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEelEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1584 EIDQLKRNHLRVVESM-QSTLDAEIRSRNDALRIKK---KMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHL 1659
Cdd:pfam02463 444 GKLTEEKEELEKQELKlLKDELELKKSEDLLKETQLvklQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1660 DDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERvqllhtqntSLINTKKKLETDISHI 1739
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGAR---------KLRLLIPKLKLPLKSI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1740 QGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEqlaLKGGKKQIQKLEA 1819
Cdd:pfam02463 595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGL---AEKSEVKASLSEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1820 RVRELENEVEGEQRRNVEAVKSLRKHERR--VKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAR 1897
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLEikKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 826320982 1898 FRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1937
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1016-1295 |
9.30e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1016 EDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlKLAQESTMDIenDKQQLDEKLKKKEFEMSNLqsk 1095
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ---RLAEYSWDEI--DVASAEREIAELEAELERL--- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1096 iEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQiemnkkREAEFQK 1175
Cdd:COG4913 681 -DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE------LRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1176 MRRDLEEatlqhEATAAALRKKHADSVAELGEQIDNLQrvkQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLE 1255
Cdd:COG4913 754 RFAAALG-----DAVERELRENLEERIDALRARLNRAE---EELERAMRAFNREWPAETADLDADLESLPEYLALLDRLE 825
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 826320982 1256 DqlSEVKTKEEEQQRLINELSaqkarlHTESGEFSRQLDE 1295
Cdd:COG4913 826 E--DGLPEYEERFKELLNENS------IEFVADLLSKLRR 857
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
912-1243 |
9.86e-08 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 57.07 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 912 KTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDD-LELTLAKVEK----EKHATENKVKNLTEEMAG 986
Cdd:pfam09731 86 KKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESatavAKEAKDDAIQAVKAHTDS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 987 LDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKA--KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLA 1064
Cdd:pfam09731 166 LKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQseEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLV 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1065 QESTMDIENDKQQLDEKLKKKE------------FEMSNLQSKIEDEQAVGMQLQKKIKELQARteeleeeiEAERASRA 1132
Cdd:pfam09731 246 DQYKELVASERIVFQQELVSIFpdiipvlkednlLSNDDLNSLIAHAHREIDQLSKKLAELKKR--------EEKHIERA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1133 kAEKQRSDLSRELEEISERLEEAGGATSAQIEmnKKREAEFQKMRRDLEE---ATLQHEATAAALRKKHADSVAELGEQI 1209
Cdd:pfam09731 318 -LEKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIELQR 394
|
330 340 350
....*....|....*....|....*....|....
gi 826320982 1210 DNLQRVKQKLEKEKSELKMEIDDLASNMETVSKA 1243
Cdd:pfam09731 395 EFLQDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1187 |
1.03e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1003 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLAQEstmDIENDK 1075
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1076 QQLDEKLKKKEFEmsNLQSKIEdeqavgmQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1155
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|..
gi 826320982 1156 GGATSAQIEmnkKREAEFQKMRRDLEEATLQH 1187
Cdd:COG1579 151 LAELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1665-1887 |
1.38e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1665 SQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEME 1744
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1745 ----DIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQL--ALKGGKKQIQKLE 1818
Cdd:COG4942 101 aqkeELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1819 ARVRELENEVEGEQRRNVEAVKSLRKherRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEA 1887
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
653-677 |
1.60e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 53.12 E-value: 1.60e-07
10 20
....*....|....*....|....*
gi 826320982 653 FRENLNKLMTNLRSTHPHFVRCIIP 677
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1388-1829 |
2.19e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 55.85 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1388 LEEAKKKLAQ---RLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEE 1464
Cdd:pfam05622 26 LQEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1465 tqaeLEASQKESRSLSTELFKVKNA-------------YEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKV 1531
Cdd:pfam05622 106 ----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1532 KKQIDQEKSELQasleEAEASLEHEEGKILRIQLELNQ-------VKSEIDRKIAEKD---EEIDQLKRNHLRVVESMQS 1601
Cdd:pfam05622 182 RGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrETNEELRCAQLQQAELSQA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1602 TLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEaiRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRAN 1681
Cdd:pfam05622 258 DALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRL--GQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRIL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1682 LMQAEVEELRASLeqtersrkmaeqelldaservQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAI 1761
Cdd:pfam05622 336 ELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 1762 TDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVE 1829
Cdd:pfam05622 395 SNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFE 470
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1372-1804 |
2.64e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 55.63 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1372 QWRTKYET-------DAIHRTEELEEAKKKLaqRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIAL 1444
Cdd:pfam06160 49 EWRKKWDDivtkslpDIEELLFEAEELNDKY--RFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1445 DKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNA--YEETLDQLETLKRENKNLQQEI----------- 1511
Cdd:pfam06160 127 KDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEELTESgdYLEAREVLEKLEEETDALEELMedipplyeelk 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1512 SDLTEQIAEGGKHIHELEKVK-----KQIDQEKSELQASLEEAEASLEheegkilriQLELNQVKSEIDrkiaEKDEEID 1586
Cdd:pfam06160 207 TELPDQLEELKEGYREMEEEGyalehLNVDKEIQQLEEQLEENLALLE---------NLELDEAEEALE----EIEERID 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1587 QLkrnhlrvvesmQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQlnhaNRQASEAIRNLR-------NTQGVLKDTQLHL 1659
Cdd:pfam06160 274 QL-----------YDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ----NKELKEELERVQqsytlneNELERVRGLEKQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1660 DDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTER-------SRKMAEQELLDASERVQLLhtqNTSLINTKKKL 1732
Cdd:pfam06160 339 EELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEeqeefkeSLQSLRKDELEAREKLDEF---KLELREIKRLV 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 826320982 1733 ETdiSHIQGEMEDIVQearnaeekakkAITDAAMMAEELKKEqdtsahLERMKKNMEQtvkdLQHRLDEAEQ 1804
Cdd:pfam06160 416 EK--SNLPGLPESYLD-----------YFFDVSDEIEDLADE------LNEVPLNMDE----VNRLLDEAQD 464
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
944-1611 |
2.69e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 56.21 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 944 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGldeNIAKLakEKKALQEAHQQTLDDLQAEEDKVNTLT 1023
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA---QINDL--EDVADKAISNDDPEEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1024 KAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKlegDLKLAQE-STMDIEndkqQLDEKLKKKEFEMSNLQSKIEDEQAV 1102
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGI---NLSYGKNlGKLFLE----KIDEEKKKSEHMIKAMEAYIEDLDEI 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1103 GMQLQKKIKELQARtEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatSAQIEMNKKREAEFQKMRRDLEE 1182
Cdd:TIGR01612 1256 KEKSPEIENEMGIE-MDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1183 ATLQHEataaalrkKHADSVAELGEQIDNLQRVKQ--KLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLED--QL 1258
Cdd:TIGR01612 1330 NLLDAQ--------KHNSDINLYLNEIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdiNL 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1259 SEVKTKEEE--QQRLINELSAQKARLHTesgefsrQLDEKEALVSQLSRGKQAFTQQIEELKRQLE-EETKAKNALAHAV 1335
Cdd:TIGR01612 1402 EECKSKIEStlDDKDIDECIKKIKELKN-------HILSEESNIDTYFKNADENNENVLLLFKNIEmADNKSQHILKIKK 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1336 QSARHDCDL----LREQYEEEQEAKAELQRG--MSKANSEVAQWRTKYETDAIHRTEELeEAKKKLAQRLQDAE----EH 1405
Cdd:TIGR01612 1475 DNATNDHDFnineLKEHIDKSKGCKDEADKNakAIEKNKELFEQYKKDVTELLNKYSAL-AIKNKFAKTKKDSEiiikEI 1553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1406 VEAVNSKCASLEKTKQRL------QNEVEDLMIDVERSNAACIALDKKQRNFDKVL---AEWKHKYEETQAELEASQKES 1476
Cdd:TIGR01612 1554 KDAHKKFILEAEKSEQKIkeikkeKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKI 1633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1477 RSLStelfkvknayeetLDQLETLKRENKNLQQEISDLTEQiaeggkhiheLEKVKKQIDQEKSElqasleeaeasLEHE 1556
Cdd:TIGR01612 1634 SSFS-------------IDSQDTELKENGDNLNSLQEFLES----------LKDQKKNIEDKKKE-----------LDEL 1679
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 1557 EGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVV-ESMQSTLDAEIRSRN 1611
Cdd:TIGR01612 1680 DSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIkELIEPTIENLISSFN 1735
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1128-1708 |
3.30e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1128 RASRAKAEKQRSDLSRELEEISerLEEAGGATSAQIEMNKKREAEFQKMRRDLEEatlQHEATAAALRkkhadsvaelgE 1207
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIE--LEKKASALKRQLDRESDRNQELQKRIRLLEK---REAEAEEALR-----------E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1208 QIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLinelsaqkarlhtesg 1287
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1288 efSRQLDEKEALVSQLSRGKQAFTQQIEELKrqlEEETKAKNaLAHAVQSARHDCDLLREQyEEEQEAKAELQRGMSKAN 1367
Cdd:pfam05557 138 --QERLDLLKAKASEAEQLRQNLEKQQSSLA---EAEQRIKE-LEFEIQSQEQDSEIVKNS-KSELARIPELEKELERLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1368 SEVAQWRTKYETDAIHRtEELEEAKKKLaqrlqdaeEHVEAVNSKCASLEKTKQRLQNEvedlmidversnaacialdkk 1447
Cdd:pfam05557 211 EHNKHLNENIENKLLLK-EEVEDLKRKL--------EREEKYREEAATLELEKEKLEQE--------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1448 qrnfdkvLAEWKHKYEETQAELEASQKESRslstelfkvknayeetldQLETLKRENKNLQQEISDLTEQiaeggkhIHE 1527
Cdd:pfam05557 261 -------LQSWVKLAQDTGLNLRSPEDLSR------------------RIEQLQQREIVLKEENSSLTSS-------ARQ 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1528 LEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQlelnqvkseidRKIAEKDEEIDQLKRNhlrvVESMQSTLDAEI 1607
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYRAI----LESYDKELTMSN 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1608 RSRNDALRIK------KKMEGDLNEMEIQLNHANRqaseairnlrnTQGVLKDTQLHLD---DAIRSQDDLKEQLAMVER 1678
Cdd:pfam05557 374 YSPQLLERIEeaedmtQKMQAHNEEMEAQLSVAEE-----------ELGGYKQQAQTLErelQALRQQESLADPSYSKEE 442
|
570 580 590
....*....|....*....|....*....|
gi 826320982 1679 RANLMQaEVEELRASLEQTERSRKMAEQEL 1708
Cdd:pfam05557 443 VDSLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1624-1937 |
3.44e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1624 LNEMEIQLNHANRQASEAIRNLrntqgvlkdtqlhlddairsqdDLKEQLAMVERRanLMQAEVEELRASLEQTERSRKM 1703
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYK----------------------ELKAELRELELA--LLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1704 AEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAitdaammAEELKKEQDTSAHLEr 1783
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL-------RERLANLERQLEELE- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1784 mkknmEQTVKDLQHRLDEAEQLAlkggkkqiqKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNV 1863
Cdd:TIGR02168 323 -----AQLEELESKLDELAEELA---------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1864 LrlqdlvdklqtkvkaykrqaeEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1937
Cdd:TIGR02168 389 A---------------------QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1455-1911 |
4.71e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1455 LAEWKHKYEETQAELEASQKESRSLSTELfkvknAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQ 1534
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1535 IDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDAL 1614
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1615 RIkkkmegDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASL 1694
Cdd:COG4717 252 LL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1695 EQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLEtdISHIQGEMEDIVQEARNAEEKakkaitDAAMMAEELKKE 1774
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEE------ELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1775 QDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALkggKKQIQKLEARVRELENEVEgeqrrnveavkslrKHERRVKELTY 1854
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELEEELEELEEELE--------------ELREELAELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1855 QTEEdrknvLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLARFRKIQHELEEAEER 1911
Cdd:COG4717 461 ELEQ-----LEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
865-1035 |
4.82e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATER-AEDEEEINAELTAKkr 943
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 944 kledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKvntLT 1023
Cdd:COG1579 90 ----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE---LE 162
|
170
....*....|..
gi 826320982 1024 KAKTKLEQQVDD 1035
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
865-1068 |
4.99e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRK 944
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 945 LEDECSEL------------------KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQ 1006
Cdd:COG4942 102 QKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 826320982 1007 QTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEST 1068
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1079-1330 |
6.00e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1079 DEKLKKKEFEMSNLQSKIEdeqavgmQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEagga 1158
Cdd:COG3883 15 DPQIQAKQKELSELQAELE-------AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1159 tsaqiemnkkREAEFQKMRRDLEEATLQHEATAAALrkkHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNME 1238
Cdd:COG3883 84 ----------RREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1239 TVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELK 1318
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|..
gi 826320982 1319 RQLEEETKAKNA 1330
Cdd:COG3883 231 AAAAAAAAAAAA 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1452-1641 |
6.49e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1452 DKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEG----GKH--- 1524
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1525 -----------------------IHELEKVKKQIDQEKSEL------QASLEEAEASLEHEEGKILRIQLELNQVKSEID 1575
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 1576 RKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEA 1641
Cdd:COG3883 175 AQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1666-1902 |
8.46e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1666 QDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRK--MAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEM 1743
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1744 EDIvQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ---TVKDLQHRLDEAEQlalkggkkQIQKLEAR 1820
Cdd:COG3206 243 AAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRA--------QLQQEAQR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1821 VR-ELENEVEGEQRRNVEAVKSLRKHERRVKELTyqteEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLARFR 1899
Cdd:COG3206 314 ILaSLEAELEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
...
gi 826320982 1900 KIQ 1902
Cdd:COG3206 390 VID 392
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1314-1889 |
9.98e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1314 IEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYE--TDAIHRTEELEEA 1391
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1392 KKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLqNEVEDLMIDVERSNAACIALDKKQ-RNFDKVLAEWK---HKYEETQA 1467
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1468 ELEASQKESrslstelfkvknayeetlDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLE 1547
Cdd:PRK01156 330 KLSVLQKDY------------------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1548 EAEASLEHEEGKILRIQLELNQVKSEIDR---KIAEKDEEIDQLKRNHLRVVESMqstldaEIRSRNDALRIKKKMEGDL 1624
Cdd:PRK01156 392 FISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNM------EMLNGQSVCPVCGTTLGEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1625 NEMEIqLNHANRQASEAIRNLRNTQGVLKDtqlhLDDAIRSQDDLKEQLAMVE-RRANLMQAEVEELRASLEQTERSrkm 1703
Cdd:PRK01156 466 KSNHI-INHYNEKKSRLEEKIREIEIEVKD----IDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIK--- 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1704 aEQELLDASERVQLLHTQNTSL-INTKKKLETDISHIQGEMEDIVQEA-RNAEEKAKKAITDAAMMAEELKKE-QDTSAH 1780
Cdd:PRK01156 538 -INELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIETnRSRSNEIKKQLNDLESRLQEIEIGfPDDKSY 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1781 LERMKKNMEQTVKDLQHRLDEAEqlALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDR 1860
Cdd:PRK01156 617 IDKSIREIENEANNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAK 694
|
570 580
....*....|....*....|....*....
gi 826320982 1861 KNVLRLQDLVDKLQTKVKAYKRQAEEAEE 1889
Cdd:PRK01156 695 ANRARLESTIEILRTRINELSDRINDINE 723
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1252-1472 |
1.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1252 RTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNAL 1331
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1332 AHAVQsarhdcDLLREQYEEEQEAKAEL---QRGMSKAN------SEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDA 1402
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLALllsPEDFLDAVrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1403 EEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEAS 1472
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1222-1580 |
1.24e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 52.62 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1222 EKSELKMEIDDLASNMETVskakgnfekmcRTLEDQLSEVKTKeeeqqrlINELSAQKARlhtesgefsrqldekealvs 1301
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKV-----------RFLEQQNKLLETK-------ISELRQKKGA-------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1302 QLSRGKQAFTQQIEELKRQLEEETKAKnalahavqsarhdcdllreqyeeeqeAKAELQRGmsKANSEVAQWRTKYETDA 1381
Cdd:pfam00038 44 EPSRLYSLYEKEIEDLRRQLDTLTVER--------------------------ARLQLELD--NLRLAAEDFRQKYEDEL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1382 IHRTeELEEAKKKLAQRLQDA-------EEHVEAVNSKCASLEKTKQ----RLQNEVEDLMIDVERSNAACIALdkkqrn 1450
Cdd:pfam00038 96 NLRT-SAENDLVGLRKDLDEAtlarvdlEAKIESLKEELAFLKKNHEeevrELQAQVSDTQVNVEMDAARKLDL------ 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1451 fDKVLAEWKHKYEEtQAELeasqkeSRSLSTELFKVKnaYEETLDQLETLKRENKNLQQEISDLTEQIAEggkHIHELEK 1530
Cdd:pfam00038 169 -TSALAEIRAQYEE-IAAK------NREEAEEWYQSK--LEELQQAAARNGDALRSAKEEITELRRTIQS---LEIELQS 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1531 VKKQidqeKSELQASLEEAEASLEHE----EGKILRIQLELNQVKSEIDRKIAE 1580
Cdd:pfam00038 236 LKKQ----KASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1574-1917 |
1.24e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1574 IDRKIAEKDEEIDQLKRNHLRVVESM--QSTLDAEIRSRNDALRIKKKMEGDLnemEIQLNH------ANRQASEAIRNL 1645
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDN---EQQTNSkdgeqlSDFQLEDLVGMI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1646 RNTQgvlKDTQLhLDDA-IRSQDDLKEQLAmvERRAnlMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTS 1724
Cdd:PLN02939 138 QNAE---KNILL-LNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1725 LINTKKKLETDISHIQGEMEDIVQEarNAEEKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNMEQTVKDLQHRLDE 1801
Cdd:PLN02939 210 LLIRGATEGLCVHSLSKELDVLKEE--NMLLKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1802 AEQLALKGGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKH---ERRVKELTYQTEEdrKNVLRLQ-DLVDKLQTKV 1877
Cdd:PLN02939 283 AQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKL 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 826320982 1878 KAYKR--QAEEAEEQSNVNL-----ARFRKIQHELEEAEERADIAES 1917
Cdd:PLN02939 361 KLLEErlQASDHEIHSYIQLyqesiKEFQDTLSKLKEESKKRSLEHP 407
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1455-1936 |
1.34e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1455 LAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQ 1534
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1535 IDQEKSELQASLEEAEASLEHeegkiLRIQLElnQVKSEIDRKIAEKDEEIDQLKRNHLRVV---ESMQSTLDAEIRSRN 1611
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEE-----LRVQAE--NARLEMHFKLKEDHEKIQHLEEEYKKEIndkEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1612 DALR----IKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEV 1687
Cdd:pfam05483 254 NKMKdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1688 EELRASLEQTERSRKMAEQELLDASERVQ-LLHTQNTSLINTKKKLETDISHIQ---GEMEDIVQEARNAE---EKAKKA 1760
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEeLLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEvelEELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1761 ITDAAMMAEELKKEQDTSahlERMKKNMEQTVKDLQHRLDEAEQLALK--GGKKQIQKLEARVRELENEVEGEQRRNVE- 1837
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1838 --------------------AVKSLRKHERRVKELTYQTEEDRKNVLRLQD----LVDKLQTKVKAYKRQAEEAEEQSNV 1893
Cdd:pfam05483 491 tahcdklllenkeltqeasdMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDK 570
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 826320982 1894 NLARFRKIQHELEEAEERADIAESQVNKLRvKSREVHTKIISE 1936
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLK-KQIENKNKNIEE 612
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
865-1077 |
1.36e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRK 944
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 945 LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDkVNTLTK 1024
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQA 958
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1025 AKTKLEQQVDDLEG-------SLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQ 1077
Cdd:TIGR02169 959 ELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
867-1326 |
1.63e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.29 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 867 KSEAKRKE-----LEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLiktkiqlEAKIKEATERAEDEEEINAELTAK 941
Cdd:pfam10174 295 KQELSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKESFLNKKTKQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 942 KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQ------TLDDLQAE 1015
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtaltTLEEALSE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1016 EDKV-NTLTKAKTKLEQQVDDlegSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQS 1094
Cdd:pfam10174 448 KERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEI 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1095 KIEDEQAVGMQLQKKIKELQarteeleeeiEAERASRAKAEkqRSDLSRELEEISERLEEAGGATSAQIE--MNKKREAE 1172
Cdd:pfam10174 525 AVEQKKEECSKLENQLKKAH----------NAEEAVRTNPE--INDRIRLLEQEVARYKEESGKAQAEVErlLGILREVE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1173 FQKMRRDLEEATLQHEATAA----------------ALRKKHADSVAELGEQIDNLQRVKQK---------LEKEKSELK 1227
Cdd:pfam10174 593 NEKNDKDKKIAELESLTLRQmkeqnkkvanikhgqqEMKKKGAQLLEEARRREDNLADNSQQlqleelmgaLEKTRQELD 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1228 MEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEV-KTKEEEQQRLINELSAQKARLHTESGEFSRQLDEkealVSQLSRG 1306
Cdd:pfam10174 673 ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEIlEMKQEALLAAISEKDANIALLELSSSKKKKTQEE----VMALKRE 748
|
490 500
....*....|....*....|
gi 826320982 1307 KQAFTQQieeLKRQLEEETK 1326
Cdd:pfam10174 749 KDRLVHQ---LKQQTQNRMK 765
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1135-1429 |
1.76e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1135 EKQRSDLSRELEEISERLEEAggatsaQIEMNKKREAEFQKMRRDLEEATLQHEAT---AAALRKKHADSVAELGEQIDN 1211
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1212 LQRVKQKLEKEK---SELKMEIDDLaSNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESG- 1287
Cdd:pfam17380 353 IRQEERKRELERirqEEIAMEISRM-RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEe 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1288 ----EFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAE----- 1358
Cdd:pfam17380 432 arqrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamiee 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1359 ------LQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAEEHveavNSKCASLEKTKQRLQNEVED 1429
Cdd:pfam17380 512 erkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE----RSRLEAMEREREMMRQIVES 584
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
846-1332 |
1.88e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 846 ETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQlqvQAEADSLADAEERCDQLIKTKIQLEAKIK--- 922
Cdd:PRK01156 239 SALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHM---KIINDPVYKNRNYINDYFKYKNDIENKKQils 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 923 ----------EATERAEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 989
Cdd:PRK01156 316 nidaeinkyhAIIKKLSVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 990 NIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEqekklrMDLERAKRKLEGDlKLAQESTM 1069
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNME------MLNGQSVCPVCGT-TLGEEKSN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1070 DI----ENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQK-----------KIKELQARTEELEEEIEAERASRAKA 1134
Cdd:PRK01156 469 HIinhyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKDKHDKY 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1135 EKQRSDL-SRELEEISERLEEAGGATSA----QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI 1209
Cdd:PRK01156 549 EEIKNRYkSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEA 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1210 DNLQRVKQklekekselkmEIDDLASNMETVSKAKGNFEKmcrtledQLSEVKTKEEEQqrliNELSAQKARLHTESGEF 1289
Cdd:PRK01156 629 NNLNNKYN-----------EIQENKILIEKLRGKIDNYKK-------QIAEIDSIIPDL----KEITSRINDIEDNLKKS 686
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 826320982 1290 SRQLD-------EKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALA 1332
Cdd:PRK01156 687 RKALDdakanraRLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
865-1070 |
2.08e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKN--DLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAkk 942
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 943 rklEDECSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLDENIAKLAKEKKALQEAhqqtldDLQAEEDKVN 1020
Cdd:COG3206 262 ---SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAALRAQLQQEAQRILASLEA------ELEALQAREA 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 826320982 1021 TLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMD 1070
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
936-1162 |
2.73e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 936 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQ-- 1013
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1014 -AEEDKVNTLTKAK--TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqestmDIENDKQQLDEKLKKKEFEMS 1090
Cdd:COG3883 99 gGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 826320982 1091 NLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1162
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1729-1892 |
2.98e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1729 KKKLETDISHIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMK-KNMEQTVKDLQHRLDEAEQLa 1806
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElQKLEKRLLQKEENLDRKLEL- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1807 LKGGKKQIQKLEARVRELENEVEgEQRRNVEavKSLRKHERRVKELTYQTEEDRKNVLrLQDLVDKLQTKVKAYKRQAE- 1885
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELE-KKEEELE--ELIEEQLQELERISGLTAEEAKEIL-LEKVEEEARHEAAVLIKEIEe 180
|
....*..
gi 826320982 1886 EAEEQSN 1892
Cdd:PRK12704 181 EAKEEAD 187
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1171-1559 |
3.23e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1171 AEFQKMRRDLEEATLQHEATAAALRKKHadsvaELGEQIDNLQRVKQKLEKEKSELKMEIDdLASNMETVSKAKGNFEkm 1250
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE-----ELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELA-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1251 crTLEDQLSEVKTKEEEQQRLINELSAQKARLHtesgEFSRQLDEKEALVSQLSRGK-QAFTQQIEELKRQLEEETKAKN 1329
Cdd:COG4717 143 --ELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1330 ALAHAVQSARHDCDLLREQYEEEQEAKaELQRGMSKANSEVAQWRTKYETDAIHRTEE------------LEEAKKKLAQ 1397
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlglLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1398 RLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHkyEETQAELEASQKESR 1477
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1478 SLST-----------ELFKVKNAYEETLDQLETLKRE----------------NKNLQQEISDLTEQIAEGGKHIHELEK 1530
Cdd:COG4717 374 ALLAeagvedeeelrAALEQAEEYQELKEELEELEEQleellgeleellealdEEELEEELEELEEELEELEEELEELRE 453
|
410 420
....*....|....*....|....*....
gi 826320982 1531 VKKQIDQEKSELQASLEEAEASLEHEEGK 1559
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
873-1084 |
3.63e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 873 KELEEKmVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEA-TERAEDEEEINAELTAKKRKLEDECSE 951
Cdd:PRK03918 518 EELEKK-AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELeEELAELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 952 LKKdIDDLELTLAKVEKEKHATENKVKNLTEEmagLDENIAKLAKEKKALQEAHQQtLDDLQAE--EDKVNTLTKAKTKL 1029
Cdd:PRK03918 597 LEP-FYNEYLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRKE-LEELEKKysEEEYEELREEYLEL 671
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1030 EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEN------DKQQLDEKLKK 1084
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlekaleRVEELREKVKK 732
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1532-1770 |
4.42e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1532 KKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID---RKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIR 1608
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAalaRRIRALEQELAALEAE-LAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1609 SRNDALRikkkmegdlnemeiqlnhanRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVE 1688
Cdd:COG4942 101 AQKEELA--------------------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1689 ELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMA 1768
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 826320982 1769 EE 1770
Cdd:COG4942 241 ER 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1491-1680 |
4.44e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1491 EETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKvkkqidqEKSELQASLEEAEASLEHEEGKILRIQLELNQv 1570
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1571 KSEIDRKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIRsrndalRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQG 1650
Cdd:COG2433 460 EIRKDREISRLDREIERLERE-LEEERERIEELKRKLE------RLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYG 532
|
170 180 190
....*....|....*....|....*....|
gi 826320982 1651 VLKDTQLHLDDAIRSQDDLKEQLAMVERRA 1680
Cdd:COG2433 533 LKEGDVVYLRDASGAGRSTAELLAEAGPRA 562
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
880-1274 |
4.50e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 880 VTLMQEKNDLQLQ----VQAEADSLADAEERCDQLiktKIQLEAK---IKEATERAEDEEEINAELTAKKRKLEDECSEL 952
Cdd:pfam15921 519 ITKLRSRVDLKLQelqhLKNEGDHLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 953 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAhqqtLDDLQAEEDKV-NTLTKAKTKLEQ 1031
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRA----VKDIKQERDQLlNEVKTSRNELNS 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1032 QVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEstmDIENDKQQLdeklkkKEFEMSNLQSKiedEQAVGMQLQ---- 1107
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS---ELEQTRNTL------KSMEGSDGHAM---KVAMGMQKQitak 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1108 -KKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ 1186
Cdd:pfam15921 740 rGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1187 ----------HEATAAALRKKHADSVAEL-GEQIDNLQRVKQKLEKEKSELKMEiDDLASNMETVSKAKGNFEKMCRTLE 1255
Cdd:pfam15921 820 faecqdiiqrQEQESVRLKLQHTLDVKELqGPGYTSNSSMKPRLLQPASFTRTH-SNVPSSQSTASFLSHHSRKTNALKE 898
|
410
....*....|....*....
gi 826320982 1256 DQLSEVKTKEEEQQRLINE 1274
Cdd:pfam15921 899 DPTRDLKQLLQELRSVINE 917
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1072-1329 |
4.55e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 51.57 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1072 ENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKEL--QARTEELEEEIEAERASRAKaekqrSDLSRELEEIS 1149
Cdd:pfam05667 211 RNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIaeQLRSAALAGTEATSGASRSA-----QDLAELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1150 ERLEEAGGATSAQiEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKME 1229
Cdd:pfam05667 286 GSSTTDTGLTKGS-RFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1230 IDDLASNMETVSK---------------------AKGNFEK---MCRTLEDQLSEVKTKEEEQQR-LINELSAQKARLHT 1284
Cdd:pfam05667 365 IKQVEEELEELKEqneelekqykvkkktldllpdAEENIAKlqaLVDASAQRLVELAGQWEKHRVpLIEEYRALKEAKSN 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 826320982 1285 ESGEFSRQLDEKEALVSQLsRGKQAFTQQIEELKRQLEEETKAKN 1329
Cdd:pfam05667 445 KEDESQRKLEEIKELREKI-KEVAEEAKQKEELYKQLVAEYERLP 488
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
982-1756 |
4.64e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 982 EEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEED---KVNTLTKAKTKLEQQVDDLEgsleqekklrmdlerakrKLE 1058
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLE------------------ELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1059 GDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIED-EQAVGMQLQKKIKELQARteeleeeieaERASRAKAEKQ 1137
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyQQALDVQQTRAIQYQQAV----------QALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1138 RSDLSreLEEISERLEEAGGATSAQIEmnKKREAEfQKMRrDLEEATLQHEATAAALRK-------KHADSVA-ELGEQI 1209
Cdd:COG3096 431 LPDLT--PENAEDYLAAFRAKEQQATE--EVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1210 DNLQRVKQKLEkeksELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQrlinELSAQKARLHTESGEF 1289
Cdd:COG3096 505 RSQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA----ELEAQLEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1290 SRQLdekealvSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHavqsarhdcdlLREQYEEEQEAKAELQRGMSK-ANS 1368
Cdd:COG3096 577 VEQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQlLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1369 EVAQWRTKYEtdAIHRTEELEEAKKKLAQ-------RLQDAEEHVEAVnskcaslektkqrLQNEVEDlmiDVERSNAAC 1441
Cdd:COG3096 639 EREATVERDE--LAARKQALESQIERLSQpggaedpRLLALAERLGGV-------------LLSEIYD---DVTLEDAPY 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1442 I-ALDKKQRNFDKV-----LAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLK-------------- 1501
Cdd:COG3096 701 FsALYGPARHAIVVpdlsaVKEQLAGLEDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgr 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1502 --RENK--NLQQEISDLTEQIAEGGKHIHELEKVKKQIDQ----------------EKSELQASLEEAEASLEHEEGKIL 1561
Cdd:COG3096 781 aaREKRleELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQ 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1562 RIQLELNQVKSEID--RKIA----------------EKDEEIDQLK---------RNHLRVVESMQSTLDAEIRSrNDAL 1614
Cdd:COG3096 861 QLRQQLDQLKEQLQllNKLLpqanlladetladrleELREELDAAQeaqafiqqhGKALAQLEPLVAVLQSDPEQ-FEQL 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1615 RIkkkmegDLNEMEIQLNHANRQA---------------SEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERR 1679
Cdd:COG3096 940 QA------DYLQAKEQQRRLKQQIfalsevvqrrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQ 1013
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1680 ANLMQAEVEELRASLEQTERSRKMAEQELLD------------ASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIV 1747
Cdd:COG3096 1014 YSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeaeerARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093
|
....*....
gi 826320982 1748 QEARNAEEK 1756
Cdd:COG3096 1094 KRLRKAERD 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1268-1520 |
6.11e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1268 QQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLRE 1347
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1348 QYEEEQEAKAELQRG---MSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQ 1424
Cdd:COG4942 98 ELEAQKEELAELLRAlyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1425 NEVEDLmidversnaacialdkkqrnfdkvlaewkhkyEETQAELEASQKESRSLSTELFKVKNAYEEtldQLETLKREN 1504
Cdd:COG4942 178 ALLAEL--------------------------------EEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEA 222
|
250
....*....|....*.
gi 826320982 1505 KNLQQEISDLTEQIAE 1520
Cdd:COG4942 223 EELEALIARLEAEAAA 238
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
848-1837 |
7.00e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 848 EKEMANMKEEFEKAKEELAKSEAKRKELeekmvtlmqeKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATER 927
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEI----------KNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 928 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVekekhatENKVKN-LTEEMAGLDENiaKLAKEKKALQEahq 1006
Cdd:TIGR01612 834 INEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAEL-------TNKIKAeISDDKLNDYEK--KFNDSKSLINE--- 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1007 qTLDDLQAEEDKVNTLtkakTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKL--KK 1084
Cdd:TIGR01612 902 -INKSIEEEYQNINTL----KKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLidKI 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1085 KEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASraKAEKQRSDLSRELEE----------------- 1147
Cdd:TIGR01612 977 NELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFD--EKEKATNDIEQKIEDanknipnieiaihtsiy 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1148 -ISERLEEAGGATSAQIEMNKKREAE-----FQKMRRDLEEATLQHEATAAALR-----KKHADSVAELGEQIDN----L 1212
Cdd:TIGR01612 1055 nIIDEIEKEIGKNIELLNKEILEEAEinitnFNEIKEKLKHYNFDDFGKEENIKyadeiNKIKDDIKNLDQKIDHhikaL 1134
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1213 QRVKQKLEKEKSELKMEIDDLASNMETvSKAKGNFEKMCRTLEDQLSEVKTKE---EEQQRLINELSaqkarlHTESGEF 1289
Cdd:TIGR01612 1135 EEIKKKSENYIDEIKAQINDLEDVADK-AISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIA------EIEKDKT 1207
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1290 SrqLDEKEALvsQLSRGKQAFTQQIEelkrQLEEETKAKNALAHAVQSARHDCDLLREQ---YEEEQEAKAELQRGMSKA 1366
Cdd:TIGR01612 1208 S--LEEVKGI--NLSYGKNLGKLFLE----KIDEEKKKSEHMIKAMEAYIEDLDEIKEKspeIENEMGIEMDIKAEMETF 1279
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1367 NSEVAQWRtKYETDAIHRTEELEEAKKKLAQRLQDaeehveavNSKCASLEKTKQRLQNEVEDlmidversnaacialdk 1446
Cdd:TIGR01612 1280 NISHDDDK-DHHIISKKHDENISDIREKSLKIIED--------FSEESDINDIKKELQKNLLD----------------- 1333
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1447 kqrnfdkvlaewkhkyeetqaeleaSQKESRSLSTELFKVKNAYeetldqlETLKREN-KNLQQEISDLTEQIAEGGKHI 1525
Cdd:TIGR01612 1334 -------------------------AQKHNSDINLYLNEIANIY-------NILKLNKiKKIIDEVKEYTKEIEENNKNI 1381
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1526 H-ELEKVKKQIDQEKSELqaSLEEAEASLEH--EEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQST 1602
Cdd:TIGR01612 1382 KdELDKSEKLIKKIKDDI--NLEECKSKIEStlDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNI 1459
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1603 LDAEIRSRNdALRIKKK-----MEGDLNEMEIQLNHANRQASEAIRNLRNTQG-------VLKDTQLHLDDaiRSQDDLK 1670
Cdd:TIGR01612 1460 EMADNKSQH-ILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkelfeqYKKDVTELLNK--YSALAIK 1536
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1671 EQLAMVERRANLMQAEVEELRASL----EQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLET------DISHIQ 1740
Cdd:TIGR01612 1537 NKFAKTKKDSEIIIKEIKDAHKKFileaEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIK 1616
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1741 GEMEDIVQEARNAEEKAKKAITDAamMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRldeaeqlalkggKKQIQKLEAR 1820
Cdd:TIGR01612 1617 KKINDCLKETESIEKKISSFSIDS--QDTELKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSE 1682
|
1050
....*....|....*..
gi 826320982 1821 VRELENEVEgEQRRNVE 1837
Cdd:TIGR01612 1683 IEKIEIDVD-QHKKNYE 1698
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1389-1584 |
7.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1389 EEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAAciaLDKKQRNFDKVLAEWKHKYEETQAE 1468
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1469 LEASQKESRSLS--TELFKVKNaYEETLDQLETLKRENKN-------LQQEISDLTEQIAEGGKHIHELEKVKKQIDQEK 1539
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSES-FSDFLDRLSALSKIADAdadlleeLKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 826320982 1540 SELQASLEEAEA---SLEHEEGKILRIQLELNQVKSEIDRKIAEKDEE 1584
Cdd:COG3883 171 AELEAQQAEQEAllaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1026-1557 |
7.68e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1026 KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLklaqestmDIENDKQQldeklkkkefemsnlqskiedeqavgmQ 1105
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQL--------DRESDRNQ---------------------------E 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1106 LQKKIKELQarteeleeeieaerasrakaekqrsdlsreleeisERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATL 1185
Cdd:pfam05557 53 LQKRIRLLE-----------------------------------KREAEAEEALREQAELNRLKKKYLEALNKKLNEKES 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1186 QhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMEtvskakgNFEKMCRTLEDQLSEVKTKE 1265
Cdd:pfam05557 98 Q-LADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-------EAEQLRQNLEKQQSSLAEAE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1266 EEQQRLINELSAQkarlhtesgefsrqldEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALahavqsaRHDCDLL 1345
Cdd:pfam05557 170 QRIKELEFEIQSQ----------------EQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN-------IENKLLL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1346 REQ----------YEEEQEAKAELQRGMSKANSEVAQWRTKYETDA--IHRTEELEEAKKKLAQRLQDAEEHVEAVNSKC 1413
Cdd:pfam05557 227 KEEvedlkrklerEEKYREEAATLELEKEKLEQELQSWVKLAQDTGlnLRSPEDLSRRIEQLQQREIVLKEENSSLTSSA 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1414 ASLEKTKQRLQNE-------VEDLMIDVERSNAACIALDK------KQRNFDKVLAEwkhKYEETQAELEASQKES---R 1477
Cdd:pfam05557 307 RQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvllltKERDGYRAILE---SYDKELTMSNYSPQLLeriE 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1478 SLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDL---------TEQIAEGGKHIHELEKVKKQIDQ---EKSELQAS 1545
Cdd:pfam05557 384 EAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLerelqalrqQESLADPSYSKEEVDSLRRKLETlelERQRLREQ 463
|
570
....*....|..
gi 826320982 1546 LEEAEASLEHEE 1557
Cdd:pfam05557 464 KNELEMELERRC 475
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1076-1238 |
9.54e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1076 QQLDEKLKKKEFEMSNLQSKIEDeqavgmqLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1155
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1156 GG-----ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEI 1230
Cdd:COG1579 86 RNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 826320982 1231 DDLASNME 1238
Cdd:COG1579 166 EELAAKIP 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1128-1370 |
1.22e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1128 RASRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAAAlrkkhaDSVAELGE 1207
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEA--------------EAALEEFRQKNGLVDLSEEAKLLL------QQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1208 QIDNLQRVKQKLEKEKSELKmeiDDLASNMETVSKAKGNFEKmcRTLEDQLSEVKTKEEEQ-----------QRLINELS 1276
Cdd:COG3206 227 QLAEARAELAEAEARLAALR---AQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELsarytpnhpdvIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1277 AQKARLHTESGefsRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAK---NALAHAVQSARHDCDLLREQYEEeq 1353
Cdd:COG3206 302 ALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESLLQRLEE-- 376
|
250
....*....|....*..
gi 826320982 1354 eakAELQRGMSKANSEV 1370
Cdd:COG3206 377 ---ARLAEALTVGNVRV 390
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
869-1336 |
1.49e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.14 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 869 EAKRKELEEKMVTLMQEKNDLQLQVqaeadsladaeercdQLIKTKIQ-----LEAKIKEATERAEDEEEINAELTAKKR 943
Cdd:pfam07111 241 ELERQELLDTMQHLQEDRADLQATV---------------ELLQVRVQslthmLALQEEELTRKIQPSDSLEPEFPKKCR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 944 KLedecseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTL- 1022
Cdd:pfam07111 306 SL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLq 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1023 ------TKAKTKLEQQVDDLEgslEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEfemsnlqski 1096
Cdd:pfam07111 380 melsraQEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVH---------- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1097 edeqavgmqlqkKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISE---RL--EEAGGATSAQIEMNKKREa 1171
Cdd:pfam07111 447 ------------TIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREernRLdaELQLSAHLIQQEVGRARE- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1172 EFQKMRRDLEEATLQHEATAaalrKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEiddLASNMETVSKAkgnfekmc 1251
Cdd:pfam07111 514 QGEAERQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQESTEEAASLRQE---LTQQQEIYGQA-------- 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1252 rtLEDQLSEVKTKEEEQ----QRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSR-GKQAFTQQIEELKRQLEEETK 1326
Cdd:pfam07111 579 --LQEKVAEVETRLREQlsdtKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRlQDEARKEEGQRLARRVQELER 656
|
490
....*....|
gi 826320982 1327 AKNALAHAVQ 1336
Cdd:pfam07111 657 DKNLMLATLQ 666
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
889-1156 |
1.56e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 889 LQLQVQAEADSLADAEER-CDQLIKT----KIQLEAKIKEATERAEDEEEINAELTAKKR----KLEDECSELKKDIDDL 959
Cdd:PHA02562 160 LDISVLSEMDKLNKDKIReLNQQIQTldmkIDHIQQQIKTYNKNIEEQRKKNGENIARKQnkydELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 960 ELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQ-----QTLDDlqaEEDKVNTLTKAKTKLEQQVD 1034
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptctQQISE---GPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1035 DLEGSLEQEKKLRMDLERAKRKLegdlklaQESTMDIENDKQQLdeklkkkefemSNLQSKIEDeqavgmqLQKKIKELQ 1114
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQSKKL-------LELKNKISTNKQSL-----------ITLVDKAKK-------VKAAIEELQ 371
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 826320982 1115 ARTEELEEEIEAERASRAKAEKQRSDLSRELEE---ISERLEEAG 1156
Cdd:PHA02562 372 AEFVDNAEELAKLQDELDKIVKTKSELVKEKYHrgiVTDLLKDSG 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
883-1061 |
1.64e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 883 MQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELT 962
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 963 LAKVEKEKHatenkVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQ 1042
Cdd:COG1579 82 LGNVRNNKE-----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170 180
....*....|....*....|
gi 826320982 1043 E-KKLRMDLERAKRKLEGDL 1061
Cdd:COG1579 157 ElEELEAEREELAAKIPPEL 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1253-1419 |
1.79e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1253 TLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAK--NA 1330
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1331 LAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQwrtkyetdaihRTEELEEAKKKLAQRLQDAEEHVEAVN 1410
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAE-----------LEAELEEKKAELDEELAELEAELEELE 162
|
....*....
gi 826320982 1411 SKCASLEKT 1419
Cdd:COG1579 163 AEREELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1488-1922 |
1.80e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1488 NAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLEL 1567
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1568 NQVKSEIDRK---IAEKDEEIDQLKRNHLRVVESMqSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRN 1644
Cdd:TIGR04523 113 KNDKEQKNKLeveLNKLEKQKKENKKNIDKFLTEI-KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1645 LRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQnts 1724
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1725 LINTKKKLETDISHIQgEMEDIVQEARNAEEKAKKaitdaammaeelKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEq 1804
Cdd:TIGR04523 269 LSEKQKELEQNNKKIK-ELEKQLNQLKSEISDLNN------------QKEQDWNKELKSELKNQEKKLEEIQNQISQNN- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1805 lalkggkKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQA 1884
Cdd:TIGR04523 335 -------KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
410 420 430
....*....|....*....|....*....|....*...
gi 826320982 1885 EEAEEQsnvnlarFRKIQHELEEAEERADIAESQVNKL 1922
Cdd:TIGR04523 408 QQKDEQ-------IKKLQQEKELLEKEIERLKETIIKN 438
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1051-1864 |
1.94e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1051 ERAKRKLEGDLKLAQE--STMDIENDKQQLDEKLKKKEFEMSNLQSKIEDE-QAV---------GMQLQKKIKELQARTE 1118
Cdd:COG3096 278 NERRELSERALELRRElfGARRQLAEEQYRLVEMARELEELSARESDLEQDyQAAsdhlnlvqtALRQQEKIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1119 ELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGG--ATSAQ-IEMNKKREAEFQKMRRDLEEATLQHEA---TAA 1192
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSqlADYQQaLDVQQTRAIQYQQAVQALEKARALCGLpdlTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1193 ALRKKHADSVAELGEQIDNLQRVKQKL--------EKEKS-ELKMEIDDLASNMETVSKAKgnfEKMCR----------- 1252
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEVLELEQKLsvadaarrQFEKAyELVCKIAGEVERSQAWQTAR---ELLRRyrsqqalaqrl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1253 -TLEDQLSEVKTKEEEQQ---RLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAK 1328
Cdd:COG3096 515 qQLRAQLAELEQRLRQQQnaeRLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1329 NALA------HAVQSARHDcdlLREQYEEEQEAKAELQRGMSK-ANSEVAQWRTKYEtdAIHRTEELEEAKKKLAQ---- 1397
Cdd:COG3096 595 KELAarapawLAAQDALER---LREQSGEALADSQEVTAAMQQlLEREREATVERDE--LAARKQALESQIERLSQpgga 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1398 ---RLQDAEEHVEAVnskcaslektkqrLQNEVEDlmiDVERSNAACI-ALDKKQRNFDKV-----LAEWKHKYEETQAE 1468
Cdd:COG3096 670 edpRLLALAERLGGV-------------LLSEIYD---DVTLEDAPYFsALYGPARHAIVVpdlsaVKEQLAGLEDCPED 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1469 LEASQKESRSLSTELFKVKNAYEETLDQLETLK----------------RENK--NLQQEISDLTEQIAEGGKHIHELEK 1530
Cdd:COG3096 734 LYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgraaREKRleELRAERDELAEQYAKASFDVQKLQR 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1531 VKKQIDQ----------------EKSELQASLEEAEASLEHEEGKILRIQLELNQVKseidrkiaekdEEIDQLKrnhlR 1594
Cdd:COG3096 814 LHQAFSQfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQLRQQLDQLK-----------EQLQLLN----K 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1595 VVESMQSTLDAEIRSRNDALRikkkmegdlNEMEIQLNHAN--RQASEAIRNLRNTQGVLKDT-------QLHLDDAIRS 1665
Cdd:COG3096 879 LLPQANLLADETLADRLEELR---------EELDAAQEAQAfiQQHGKALAQLEPLVAVLQSDpeqfeqlQADYLQAKEQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1666 QDDLKEQL-AM---VERRANLMQAE-----------VEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKK 1730
Cdd:COG3096 950 QRRLKQQIfALsevVQRRPHFSYEDavgllgensdlNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRD 1029
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1731 -KLETdISHIQGEMEDI-VQEARNAEEKAKkaitdaammaeELKKEQDTSAHLERMKKNmeQTVKDLQHRldEAEqlalk 1808
Cdd:COG3096 1030 aKQQT-LQELEQELEELgVQADAEAEERAR-----------IRRDELHEELSQNRSRRS--QLEKQLTRC--EAE----- 1088
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1809 ggkkqIQKLEARVRELENEVEGEQRRNVEAVKS------LRKH---ERRV--KELTYQTEEDRKNVL 1864
Cdd:COG3096 1089 -----MDSLQKRLRKAERDYKQEREQVVQAKAGwcavlrLARDndvERRLhrRELAYLSADELRSMS 1150
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1755-1927 |
1.95e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1755 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLalkggkKQIQKLEARVRELENEVEGEQRR 1834
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1835 nveaVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQA-EEAEEQSNVNLARFRKIQHELEEAEERAD 1913
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....
gi 826320982 1914 IAESQVNKLRVKSR 1927
Cdd:COG4717 224 ELEEELEQLENELE 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
799-1327 |
1.97e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 799 MRVEFRKMMERRESIFCIQYNIRAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKAKEELAKSEAKrKELEEK 878
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGA-TAVYSQ 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 879 MVTLMQEKNDLQLQVqaeadsladaeerCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDD 958
Cdd:TIGR00606 668 FITQLTDENQSCCPV-------------CQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 959 LELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKlakekkalqeaHQQTLDDLQAEEDKVNTLTKAKTKLEQqvddleg 1038
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-----------QETLLGTIMPEEESAKVCLTDVTIMER------- 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1039 sleqekkLRMDLERAKRKLEGdlKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTe 1118
Cdd:TIGR00606 797 -------FQMELKDVERKIAQ--QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT- 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1119 eleEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATaaalRKKH 1198
Cdd:TIGR00606 867 ---NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS----NKKA 939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1199 ADSVAELGEQIDNL--------QRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEdqlSEVKTKEEEQQR 1270
Cdd:TIGR00606 940 QDKVNDIKEKVKNIhgymkdieNKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR---QDIDTQKIQERW 1016
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1271 LINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKA 1327
Cdd:TIGR00606 1017 LQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLA 1073
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1463-1804 |
2.25e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1463 EETQAELEASQKeSRSLSTELFKVKNAYEETLDQL---ETLKRENKNLQQEISDLTEQIAEGGKhihELEKVKKQIDQEK 1539
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1540 SE--LQASLEEAEASLEHEEGKILRIQLELNQVKSEIdrkiaekdeeIDQLKRNhlrvvESMQSTLDAEIrSRNDALRIK 1617
Cdd:PRK11281 115 REtlSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQL----------VSLQTQP-----ERAQAALYANS-QRLQQIRNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1618 KKmegdlnemeiqlnhANRQASEAirnLRNTQGVLKDTQLHLDDAirsQDDLKEQLAmveRRANLMQaeveelraSLEQT 1697
Cdd:PRK11281 179 LK--------------GGKVGGKA---LRPSQRVLLQAEQALLNA---QNDLQRKSL---EGNTQLQ--------DLLQK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1698 ERSRKMAEQELLDasERVQLLHTqntsLINTKKKLETdishiqgemEDIVQEARNAEEKAKkaITDAAMMAEELKKEQDT 1777
Cdd:PRK11281 228 QRDYLTARIQRLE--HQLQLLQE----AINSKRLTLS---------EKTVQEAQSQDEAAR--IQANPLVAQELEINLQL 290
|
330 340 350
....*....|....*....|....*....|
gi 826320982 1778 SAHLERMKKNMEQTVKD---LQHRLDEAEQ 1804
Cdd:PRK11281 291 SQRLLKATEKLNTLTQQnlrVKNWLDRLTQ 320
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
929-1341 |
2.51e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 929 EDEEEINAELTAKKRKLEDeCSELKKD----IDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeniaklakekkALQEA 1004
Cdd:pfam19220 3 QRNELLRVRLGEMADRLED-LRSLKADfsqlIEPIEAILRELPQAKSRLLELEALLAQERAAYG-----------KLRRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1005 HQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKK 1084
Cdd:pfam19220 71 LAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1085 KEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLeeaggatsaqie 1164
Cdd:pfam19220 151 AEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQL------------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1165 MNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIdnLQRVKQKLeKEKSElkmEIDDLASNMETVSKAK 1244
Cdd:pfam19220 219 AAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQL--LAEARNQL-RDRDE---AIRAAERRLKEASIER 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1245 GNFEKMCRTLEDQLS--EVKTKEEEQQR---------LINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQ 1313
Cdd:pfam19220 293 DTLERRLAGLEADLErrTQQFQEMQRARaeleeraemLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQA 372
|
410 420
....*....|....*....|....*....
gi 826320982 1314 IEELKRQLEEEtKAKNALAH-AVQSARHD 1341
Cdd:pfam19220 373 NRRLKEELQRE-RAERALAQgALEIARES 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1502-1937 |
2.96e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1502 RENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKilriqlelnqvKSEIDRKIAEK 1581
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-----------KAEDARKAEEA 1145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1582 DEEIDQLKRNHLRVVESMQSTldAEIRSRNDAlrikKKMEGDLNEMEIQLNHANRQASEAirnlRNTQGVLKDTQLHLDD 1661
Cdd:PTZ00121 1146 RKAEDAKRVEIARKAEDARKA--EEARKAEDA----KKAEAARKAEEVRKAEELRKAEDA----RKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1662 AIRSQDDLKEQLAMveRRANLMQAEVEELRASLEQ--TERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHI 1739
Cdd:PTZ00121 1216 EARKAEDAKKAEAV--KKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1740 Q---GEMEDIVQEARNAEEKAKKAiTDAAMMAEELKKEQDTsahlerMKKNMEQTVKDlqhrlDEAEQLALKGGKKQIQK 1816
Cdd:PTZ00121 1294 EakkAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADA------AKKKAEEAKKA-----AEAAKAEAEAAADEAEA 1361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1817 LEARVRELENEVEgEQRRNVEAVKSLRKHERRVKELTYQTEEDRKnvlRLQDLVDKLQTKVKA--YKRQAEEAEEQSNV- 1893
Cdd:PTZ00121 1362 AEEKAEAAEKKKE-EAKKKADAAKKKAEEKKKADEAKKKAEEDKK---KADELKKAAAAKKKAdeAKKKAEEKKKADEAk 1437
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 826320982 1894 NLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1937
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1684-1911 |
3.18e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1684 QAEVEELRASLEQTERSRKmaEQELLDASERVQLLHTQNTSlintKKKLETDISHIQgEMEDIVQEARNAEEKAKKAITD 1763
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK--QMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1764 AAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRL-DEAEQLalkggKKQIQKLEARVRELENEVEGEQRRNVEAVKSL 1842
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1843 RKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVkaykrQAEEAEEQSNVNLARFRKIQHELEEAEER 1911
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1659-1937 |
3.57e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1659 LDDAIRSQDDLKEQLAMVER-----RANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLlHTQNTSLINTkkkLE 1733
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELET---LE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1734 TDIShiqgEMEDIVQEARNAEEKAKKAITDAAMMAEELKKE-QDTSAHLErmkknmeqtvkdlqhrLDEAEQLALKggkK 1812
Cdd:PRK02224 258 AEIE----DLRETIAETEREREELAEEVRDLRERLEELEEErDDLLAEAG----------------LDDADAEAVE---A 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1813 QIQKLEARVRELENEVEgEQRRNVEAVKSLRKHER-RVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQS 1891
Cdd:PRK02224 315 RREELEDRDEELRDRLE-ECRVAAQAHNEEAESLReDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 826320982 1892 NVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1937
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1536-1716 |
4.27e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1536 DQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDR---KIAEKDEEIDQLKRNhlrvVESMQSTLDAEIRSRND 1612
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAE----IAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1613 ALRIKKKMEGDLNEMEI---------------QLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVE 1677
Cdd:COG3883 91 RARALYRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 826320982 1678 RRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQ 1716
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1483-1929 |
4.44e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 48.31 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1483 LFKVKNAYEEtLDQLETLKRE--NKNLQQEISDLtEQIAEGGKHIHELEKVKKQ----IDQEKSELQASLEEAEASLEhe 1556
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1557 EGKILRIQLELNQVKS---EIDRKIAEKDEEIDQL----KRNHLRV--VESMQSTLDAEIRSRNDAL-RIKKKMEGDLNE 1626
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELleseEKNREEVeeLKDKYRELRKTLLANRFSYgPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1627 MEIQLNHANRqaseairnlRNTQGVLKDTQLHLDDAIRSQDDLKEQL----AMVERRANLMQAEVEELRASLeqtersRK 1702
Cdd:pfam06160 158 IEEEFSQFEE---------LTESGDYLEAREVLEKLEEETDALEELMedipPLYEELKTELPDQLEELKEGY------RE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1703 MAEQ----ELLDASERVQLLHTQNTSLINTKKKLETD-----ISHIQGEMEDIvQEARNAEEKAKKaitdaammaeELKK 1773
Cdd:pfam06160 223 MEEEgyalEHLNVDKEIQQLEEQLEENLALLENLELDeaeeaLEEIEERIDQL-YDLLEKEVDAKK----------YVEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1774 EQDT-SAHLERMKKNMEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELENEVEGEQRRNV-------EAVK 1840
Cdd:pfam06160 292 NLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSelqeeleEILE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1841 SLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAE----------------EAEEQSNVNLARFRKIQHE 1904
Cdd:pfam06160 372 QLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADELNEVPLN 451
|
490 500
....*....|....*....|....*
gi 826320982 1905 LEEAEERADIAESQVNKLRVKSREV 1929
Cdd:pfam06160 452 MDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1497-1937 |
4.81e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1497 LETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASL--------EEAEASLEHEEGKILRIQLELN 1568
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1569 QVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNT 1648
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1649 QGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINT 1728
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1729 KKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALK 1808
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1809 GGKKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAE 1888
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 826320982 1889 EQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1937
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1327-1520 |
4.85e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1327 AKNALAHAVQSARHDCDLLREqyEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTEELEEAKKKLAQRlqdaeehV 1406
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1407 EAVNSKCASLEKTKQRLQNEVEDlmidversnaaciaLDKKQRNFDKVLAEWKHKYEETQAELEasqkESRSLSTElfkv 1486
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKE--------------LEQKQQELEKKEEELEELIEEQLQELE----RISGLTAE---- 153
|
170 180 190
....*....|....*....|....*....|....
gi 826320982 1487 kNAYEETLDQLEtlkrenKNLQQEISDLTEQIAE 1520
Cdd:PRK12704 154 -EAKEILLEKVE------EEARHEAAVLIKEIEE 180
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
945-1228 |
5.01e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 945 LEDECSELKKDIDDLELTLAKVEkEKHATENKvkNLTEEMAGLDENIAklakEKKALQEAHQQTLDDLQAEEDKVNTltk 1024
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQ-QQIKTYNK--NIEEQRKKNGENIA----RKQNKYDELVEEAKTIKAEIEELTD--- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1025 AKTKLEQQVDDLEGSLeqeKKLRMDLERAKRKLEgdlKLAQESTMDIEND-----KQQL---DEKLKKKEFEMSNLQSKI 1096
Cdd:PHA02562 242 ELLNLVMDIEDPSAAL---NKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQIsegPDRITKIKDKLKELQHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1097 EDeqavgmqLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEiserleeaggatsaqiemNKKREAEFQKm 1176
Cdd:PHA02562 316 EK-------LDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK------------------AKKVKAAIEE- 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 826320982 1177 rrdleeatlqheatAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKM 1228
Cdd:PHA02562 370 --------------LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
962-1193 |
6.36e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 962 TLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDdlegslE 1041
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE------E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1042 QEKKLRMDLERAKRKLEGDLKLAQ----ESTMD-----------IENDKQQLDEkLKKKEFEMSNLQSKIEDEQAvgmQL 1106
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsESFSDfldrlsalskiADADADLLEE-LKADKAELEAKKAELEAKLA---EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1107 QKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ 1186
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
....*..
gi 826320982 1187 HEATAAA 1193
Cdd:COG3883 240 AAAAASA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1729-1928 |
6.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1729 KKKLETDISHIQGEMEDIVqEARNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKK-----NMEQTVKDLQHRLD 1800
Cdd:COG4913 220 EPDTFEAADALVEHFDDLE-RAHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1801 EAEQlALKGGKKQIQKLEARVRELENEVEG--EQRRNV--EAVKSLrkhERRVKELTYQTEEDRKNVLRLQDLVDKLQTK 1876
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDEleAQIRGNggDRLEQL---EREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 826320982 1877 VKAYKRQAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNK-LRVKSRE 1928
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRReLRELEAE 427
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1254-1520 |
7.41e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 47.92 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1254 LEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAH 1333
Cdd:pfam09726 407 LKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEK 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1334 AVQSARHdcdllREQYEEEQEAKAELQRGMSKANSevaqwrtkyeTDAI-HRTEELEEAKKKLAQRLQDAEEHVEAVNSK 1412
Cdd:pfam09726 487 QLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQIRELEIK 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1413 CASLEKTKQRlQNEVEDLMidversnAACIALDKKQRNFDKVLAewkhkyEETQAELeasqkesrslstELFkvkNAYEE 1492
Cdd:pfam09726 552 VQELRKYKES-EKDTEVLM-------SALSAMQDKNQHLENSLS------AETRIKL------------DLF---SALGD 602
|
250 260
....*....|....*....|....*...
gi 826320982 1493 TLDQLETLKRENKNLQQEISDLTEQIAE 1520
Cdd:pfam09726 603 AKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
891-1032 |
7.83e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 891 LQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEI---NAELTAKKRKLEDECSELKKDIDDLeltlakvE 967
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEKRLLQKEENLDRKLELL-------E 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 968 KEKHATENKVKNLTEEMagldENIAKLAKEKKALQEAHQQTLDD---LQAEEDKVNTLTKAKTKLEQQ 1032
Cdd:PRK12704 107 KREEELEKKEKELEQKQ----QELEKKEEELEELIEEQLQELERisgLTAEEAKEILLEKVEEEARHE 170
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
834-1733 |
1.03e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 834 LYFKIKPLLKS-AETEKEMA--------NMKEEFEKAKEELAKSEAKRKELE---EKMVTLMQEKNDLQLQVQAEADSLA 901
Cdd:TIGR01612 1188 IYDEIKKLLNEiAEIEKDKTsleevkgiNLSYGKNLGKLFLEKIDEEKKKSEhmiKAMEAYIEDLDEIKEKSPEIENEMG 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 902 DAEERCDQLIKTKIQLEAKIKEATERAEDEEEInAELTAKKRKLEDECSElKKDIDDLELTLAK--VEKEKHATE----- 974
Cdd:TIGR01612 1268 IEMDIKAEMETFNISHDDDKDHHIISKKHDENI-SDIREKSLKIIEDFSE-ESDINDIKKELQKnlLDAQKHNSDinlyl 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 975 NKVKNLTeemagldeNIAKLAKEKKALQEAHQQTLD------DLQAEEDKVNTLTKA----------KTKLEQQVD--DL 1036
Cdd:TIGR01612 1346 NEIANIY--------NILKLNKIKKIIDEVKEYTKEieennkNIKDELDKSEKLIKKikddinleecKSKIESTLDdkDI 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1037 EGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIendkqqldeKLKKKEFEMSNLQSkiedeqavgmQLQKKIKELQAR 1116
Cdd:TIGR01612 1418 DECIKKIKELKNHILSEESNIDTYFKNADENNENV---------LLLFKNIEMADNKS----------QHILKIKKDNAT 1478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1117 teeleeeieaerasrakaekqrSDLSRELEEISERLEEAGG------ATSAQIEMNKKReaeFQKMRRDLEEatLQHEAT 1190
Cdd:TIGR01612 1479 ----------------------NDHDFNINELKEHIDKSKGckdeadKNAKAIEKNKEL---FEQYKKDVTE--LLNKYS 1531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1191 AAALRKKHADSVAELGEQIDNLQRVKQK--LEKEKSELKME--------IDDLASNMETVSKAKGNFEKMCRTLEDQL-- 1258
Cdd:TIGR01612 1532 ALAIKNKFAKTKKDSEIIIKEIKDAHKKfiLEAEKSEQKIKeikkekfrIEDDAAKNDKSNKAAIDIQLSLENFENKFlk 1611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1259 -SEVKTK-------EEEQQRLINELSaqkarLHTESGEFSRQLDEKEALvsqlsrgkQAFTQQIEELKRQLEEETKAKNA 1330
Cdd:TIGR01612 1612 iSDIKKKindclkeTESIEKKISSFS-----IDSQDTELKENGDNLNSL--------QEFLESLKDQKKNIEDKKKELDE 1678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1331 LAHAVQSARHDCDLLREQYE---------EEQEAKAELQRGMSKANSEVAQWRTKYET---DAIHRTEELEEAKKKLAQR 1398
Cdd:TIGR01612 1679 LDSEIEKIEIDVDQHKKNYEigiiekikeIAIANKEEIESIKELIEPTIENLISSFNTndlEGIDPNEKLEEYNTEIGDI 1758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1399 LqdaEEHVEAVNSKCASLEKTKQR--LQNEVEDLMIDVERSNAACIALDKKQRN---------FDKVLAEWKHKYEETQA 1467
Cdd:TIGR01612 1759 Y---EEFIELYNIIAGCLETVSKEpiTYDEIKNTRINAQNEFLKIIEIEKKSKSylddieakeFDRIINHFKKKLDHVND 1835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1468 eleasqkesrSLSTELFKVKNAYEETLDQLETLKRE-NKNLQQEISDLTEQIAEG--GKHIHELEKVKKQIDQEKSELQA 1544
Cdd:TIGR01612 1836 ----------KFTKEYSKINEGFDDISKSIENVKNStDENLLFDILNKTKDAYAGiiGKKYYSYKDEAEKIFINISKLAN 1905
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1545 SLEeaeasleheegkilrIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQ--STLDAEIR-SRNDALRIKKKME 1621
Cdd:TIGR01612 1906 SIN---------------IQIQNNSGIDLFDNINIAILSSLDSEKEDTLKFIPSPEkePEIYTKIRdSYDTLLDIFKKSQ 1970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1622 gDLNEMEIQ---LNHANRQASEAIRNLRNTQGVLKDTQ-------------LHLDDAIR----------------SQDDL 1669
Cdd:TIGR01612 1971 -DLHKKEQDtlnIIFENQQLYEKIQASNELKDTLSDLKykkekilndvkllLHKFDELNklscdsqnydtilelsKQDKI 2049
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 1670 KEQLAMVERR---------ANLMQAEVEELRASLEQTERSRKMAEQELLDASErvqllhtQNTSLINTKKKLE 1733
Cdd:TIGR01612 2050 KEKIDNYEKEkekfgidfdVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSE-------EKDNIIQSKKKLK 2115
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
950-1155 |
1.13e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.00 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 950 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDL----------------- 1012
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAfrqgehtglqlilsgee 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1013 ---------------QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEN---- 1073
Cdd:PRK11637 151 sqrgerilayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqk 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1074 DKQQLDEkLKKKEfemSNLQSKIedeqavgmqlqkkikelqARTeeleeeieaERASRAKAEKQrsdlSRELEEISERLE 1153
Cdd:PRK11637 231 DQQQLSE-LRANE---SRLRDSI------------------ARA---------EREAKARAERE----AREAARVRDKQK 275
|
..
gi 826320982 1154 EA 1155
Cdd:PRK11637 276 QA 277
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1033-1398 |
1.18e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1033 VDDLEGSLeqeKKLRMDLE--RAKRKLEGDLK-LAQEST-------MDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAV 1102
Cdd:PRK04863 232 FQDMEAAL---RENRMTLEaiRVTQSDRDLFKhLITESTnyvaadyMRHANERRVHLEEALELRRELYTSRRQLAAEQYR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1103 GMQLQKKIKELQARTEELEEEIEAERASRAK---AEKQRSDLSR---ELEEISERLEEAGGATSAQIEMNKKREAEFQKM 1176
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYQAASDHLNLvqtALRQQEKIERyqaDLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1177 RRDLEEATLQ------------------HEATAAALRKKHADSVAELGeqIDNLQRVKQKLEKEKSELKMEIDDLASNME 1238
Cdd:PRK04863 389 EEEVDELKSQladyqqaldvqqtraiqyQQAVQALERAKQLCGLPDLT--ADNAEDWLEEFQAKEQEATEELLSLEQKLS 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1239 TVSKAKGNFEKMCRTLedqlsevktkeeeqQRLINELSAQKArlHTESGEFSRQLDEKEALVSQLsrgkQAFTQQIEELK 1318
Cdd:PRK04863 467 VAQAAHSQFEQAYQLV--------------RKIAGEVSRSEA--WDVARELLRRLREQRHLAEQL----QQLRMRLSELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1319 RQLEEETKAKNALAHAVQSARHDCDlLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYEtdaiHRTEELEEAKKKLAQR 1398
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLD-DEDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQLQARIQRLAAR 601
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1748-1937 |
1.24e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1748 QEARNAEE----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAE------QLALKGGKKQIQKL 1817
Cdd:COG1196 207 RQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEaeleelRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1818 EARVRELENEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAR 1897
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 826320982 1898 FRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1937
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1384-1912 |
1.24e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1384 RTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYE 1463
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1464 ETQAELEaSQKESRSLSTELFKVKNAYEEtldqLETLKRENKNLQQEIsDLTEQIAEGGKHIHELEKVKKQIDQEKSELQ 1543
Cdd:TIGR00618 244 YLTQKRE-AQEEQLKKQQLLKQLRARIEE----LRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1544 ASLEEAEASLEHEEgkilriqlelNQVKSEIDRKIAEKDEEIDQLKRNHLRVvESMQSTLDAEIRSRNDALRIKKKMEGD 1623
Cdd:TIGR00618 318 SKMRSRAKLLMKRA----------AHVKQQSSIEEQRRLLQTLHSQEIHIRD-AHEVATSIREISCQQHTLTQHIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1624 LNEMEIQLNHANRQASEAIRNLRNTQgvlkDTQLhlddaiRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKM 1703
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATI----DTRT------SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1704 AEQELLDASERVQLLHTQNTSLINTKKKlETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1783
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1784 MKKNMEQTVKDLQHRLDEAeqlalkggKKQIQKLEARVRELENEvegeqrrnveavksLRKHERRVKELTYQTEEDRKNV 1863
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSE--------RKQRASLKEQMQEIQQS--------------FSILTQCDNRSKEDIPNLQNIT 593
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 826320982 1864 LRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLARFRKIQHELEEAEERA 1912
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
892-1144 |
1.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 892 QVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDeeeinaeltakkrkLEDECSELKKDIDDLELTLAKVEKEKH 971
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 972 ATENKVKNLTEEMAGLDENIAKLAkekkALQEAhqQTLDDLQAEEDKVNTLTKAKTKLeqqvddlegsLEQEKKLRMDLE 1051
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLD----VLLGS--ESFSDFLDRLSALSKIADADADL----------LEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1052 RAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEEIEAERASR 1131
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|...
gi 826320982 1132 AKAEKQRSDLSRE 1144
Cdd:COG3883 227 AAAAAAAAAAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1566-1809 |
1.28e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1566 ELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQStLDAEIRSRNDALRikkKMEGDLNEMEIQLNHANRQASEAIRNL 1645
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIR---ALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1646 RNTQGVLKDtQLHLDDAIRSQDDLK-----EQLAMVERRANLMQAEVEELRASLEQTERSRkmaeqelldaservQLLHT 1720
Cdd:COG4942 100 EAQKEELAE-LLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADL--------------AELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1721 QNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLD 1800
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*....
gi 826320982 1801 EAEQLALKG 1809
Cdd:COG4942 245 AAGFAALKG 253
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1377-1619 |
1.76e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.75 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1377 YETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKcASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNfdkvla 1456
Cdd:NF012221 1529 YILDNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALE------ 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1457 ewkhkyEETQAELEASQKESRSLSTELFKVKnayeETLDQLETLKRENKNLQQE---------ISDLTEQIAEGGKHIHE 1527
Cdd:NF012221 1602 ------TNGQAQRDAILEESRAVTKELTTLA----QGLDALDSQATYAGESGDQwrnpfagglLDRVQEQLDDAKKISGK 1671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1528 -LEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKiaeKDEEIDQLKRNHLRVVESMQSTLDAE 1606
Cdd:NF012221 1672 qLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR---KDDALAKQNEAQQAESDANAAANDAQ 1748
|
250
....*....|...
gi 826320982 1607 IRSRNDALRIKKK 1619
Cdd:NF012221 1749 SRGEQDASAAENK 1761
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1313-1553 |
1.87e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 45.48 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1313 QIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVaqwrtkyeTDAIHRTEELEEAK 1392
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAES--------ERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1393 KKLAQRLQDAEEHVEAVNSKCASL-EKTKQRLQNEVEDLMIDVERSNaaciaLDKKQRNFDKVLAEWKHKYEETQAELEA 1471
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1472 SQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTeqiAEGGKHIHELEKVKKQIDQEKSELQASLEEAEA 1551
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 826320982 1552 SL 1553
Cdd:pfam06008 244 SL 245
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1133-1324 |
1.98e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1133 KAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKmrrDLEEATLQHEataaalrkkhaDSVAELGEQIDNL 1212
Cdd:PRK05771 47 KLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIE-----------KEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1213 QRVKQKLEKEKSELK------MEIDDLASNmETVS-----KAKGNFEKMCRTLEDQ----LSEVKTK-----------EE 1266
Cdd:PRK05771 113 ENEIKELEQEIERLEpwgnfdLDLSLLLGF-KYVSvfvgtVPEDKLEELKLESDVEnveyISTDKGYvyvvvvvlkelSD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1267 EQQRLINELSAQKARLhTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEE 1324
Cdd:PRK05771 192 EVEEELKKLGFERLEL-EEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEE 248
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
914-1099 |
2.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 914 KIQLEAKIKEATERAE---DEEEINAELTAKKRKLedecsELKKDIDDLEltlAKVEKEKHATENKVKNLteemaglden 990
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALL-----EAKEEIHKLR---NEFEKELRERRNELQKL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 991 iaklakEKKALQeaHQQTLDdlqaeeDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdLKLAQESTMD 1070
Cdd:PRK12704 88 ------EKRLLQ--KEENLD------RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL--QELERISGLT 151
|
170 180 190
....*....|....*....|....*....|
gi 826320982 1071 IENDKQQLDEKLKKK-EFEMSNLQSKIEDE 1099
Cdd:PRK12704 152 AEEAKEILLEKVEEEaRHEAAVLIKEIEEE 181
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
835-1410 |
2.36e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 835 YFKIKPLLKSAETE-KEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEE---RCDQL 910
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalnELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 911 IKTKIQLEAKIKEATERAEDEEEINAELTA--------------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK 976
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKEleerhmkiindpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 977 VKNLTEEMAGLDENIaklakEKKALQEAHQQTLDDLQAEEDKVNTLTKaktkleqQVDDLEGSLEQEKKlrmDLERAKRK 1056
Cdd:PRK01156 328 IKKLSVLQKDYNDYI-----KKKSRYDDLNNQILELEGYEMDYNSYLK-------SIESLKKKIEEYSK---NIERMSAF 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1057 LEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTE-ELEEEIEAERASRAKAE 1135
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcPVCGTTLGEEKSNHIIN 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1136 KQRSDLSRELEEISErLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDnlqrv 1215
Cdd:PRK01156 473 HYNEKKSRLEEKIRE-IEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHD----- 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1216 kqKLEKEKSELK-MEIDDLASNMETVSKAKGNFEKM-CRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQL 1293
Cdd:PRK01156 547 --KYEEIKNRYKsLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREI 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1294 DEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAknalAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQW 1373
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQ----IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARL 700
|
570 580 590
....*....|....*....|....*....|....*..
gi 826320982 1374 RTKYETDaIHRTEELEEAKKKLAQRLQDAEEHVEAVN 1410
Cdd:PRK01156 701 ESTIEIL-RTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1669-1937 |
2.65e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1669 LKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKklETDISHIQGEMEDIVQ 1748
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ--ERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1749 EARNAEEKAkkaitdaaMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEV 1828
Cdd:pfam17380 356 EERKRELER--------IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1829 EGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRL-QDLVDKLQTKVKAYKRQAE--EAEEQSnvnlarfRKIQHEL 1905
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrQQEEERKRKKLELEKEKRDrkRAEEQR-------RKILEKE 500
|
250 260 270
....*....|....*....|....*....|..
gi 826320982 1906 EEAEERADIAESQVNKLRVKSREVHTKIISEE 1937
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1751-1916 |
2.92e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1751 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTVKDLQHRLdeaeqlalkggkkqIQKLEARVRELENEVEG 1830
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKL--------------RNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1831 EQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKV-KAYKRQAEEAEEQSNVNLARFRKIQHELEEAE 1909
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELeELIEEQLQELERISGLTAEEAKEILLEKVEEE 166
|
....*..
gi 826320982 1910 ERADIAE 1916
Cdd:PRK12704 167 ARHEAAV 173
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1294-1557 |
3.16e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1294 DEKEALVSQLsRGKQAFtqQIEELKRQLEEEtKAKNALAHAVQSARHdCDLLReQYEEEQEAKAELQRGMSKansevaqw 1373
Cdd:PRK05771 16 SYKDEVLEAL-HELGVV--HIEDLKEELSNE-RLRKLRSLLTKLSEA-LDKLR-SYLPKLNPLREEKKKVSV-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1374 rtkyetdaihrtEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLM----IDVErsnaacIALDKKQR 1449
Cdd:PRK05771 82 ------------KSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnFDLD------LSLLLGFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1450 NFdKVLAEWKHKYEETQAELEASQKESRSLSTE-------LFKVKNAYEETLDQLETLKRENKNL------QQEISDLTE 1516
Cdd:PRK05771 144 YV-SVFVGTVPEDKLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFERLELeeegtpSELIREIKE 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 826320982 1517 QIAEggkhIH-ELEKVKKQI----DQEKSELQASLEEAEASLEHEE 1557
Cdd:PRK05771 223 ELEE----IEkERESLLEELkelaKKYLEELLALYEYLEIELERAE 264
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
868-1557 |
3.53e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 868 SEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLaDAEERCDQLiktkiQLEAKIKEATERAEDEEEINAELTAKKRKLED 947
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSL-NWLTRLDEL-----QQEASRRQQALQQALAAEEKAQPQLAALSLAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 948 ECSELKKDIDDLELTLAKVEKEKHATEnKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKV----NTLT 1023
Cdd:PRK10246 288 PARQLRPHWERIQEQSAALAHTRQQIE-EVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFrqwnNELA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1024 KAKTKLEQQVDDLEgsleQEKKLRMDLERAKRKLEG----DLKLAQEST---MDIENDKQQLDEKLkkkefemSNLQSKI 1096
Cdd:PRK10246 367 GWRAQFSQQTSDRE----QLRQWQQQLTHAEQKLNAlpaiTLTLTADEVaaaLAQHAEQRPLRQRL-------VALHGQI 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1097 EDEQAVGMQLQKKIKELQARTEELEEEIEAERAS---------RAKAEKQRSDLSRELEEISERLEEA------GGATSA 1161
Cdd:PRK10246 436 VPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRykektqqlaDVKTICEQEARIKDLEAQRAQLQAGqpcplcGSTSHP 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1162 QIEMNKKREAEFQKMRRDL---EEATLQHEatAAALRKkhadsvaelgeQIDNLQRVKQKLEKEKSELKMEIDDLASNME 1238
Cdd:PRK10246 516 AVEAYQALEPGVNQSRLDAlekEVKKLGEE--GAALRG-----------QLDALTKQLQRDESEAQSLRQEEQALTQQWQ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1239 TVSKAKGnfekMCRTLEDQLSEVKTKEEEQQRLINELSaQKARLHTesgefsrQLDEKEALVSQlsrgkqaFTQQIEELK 1318
Cdd:PRK10246 583 AVCASLN----ITLQPQDDIQPWLDAQEEHERQLRLLS-QRHELQG-------QIAAHNQQIIQ-------YQQQIEQRQ 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1319 RQLEeetkakNALAHAVQSARHDCDLLREQYEEEQEAK------AELQRGMSKANSEVAQWRTKYETDaihrtEELEEAK 1392
Cdd:PRK10246 644 QQLL------TALAGYALTLPQEDEEASWLATRQQEAQswqqrqNELTALQNRIQQLTPLLETLPQSD-----DLPHSEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1393 KKLAQRLQDAEEhveavnsKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDK--VLA-----EWKHKYEET 1465
Cdd:PRK10246 713 TVALDNWRQVHE-------QCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQqaFLAalldeETLTQLEQL 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1466 QAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQAS 1545
Cdd:PRK10246 786 KQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQAL 865
|
730
....*....|...
gi 826320982 1546 LEE-AEASLEHEE 1557
Cdd:PRK10246 866 MQQiAQATQQVED 878
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1748-1913 |
4.08e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1748 QEARNAEEKAKKAITDAAMMAEELKKEQDTSA--HLERMKKNMEQTVKDLQHRLDEAEqlalkggkkqiQKLEARVRELE 1825
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEKELRERRNELQKLE-----------KRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1826 NEVEGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVlrlQDLVDKLQ-----TKVKAYKRQAEEAEEQSNVNLARFrk 1900
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI---EEQLQELErisglTAEEAKEILLEKVEEEARHEAAVL-- 174
|
170
....*....|...
gi 826320982 1901 IQHELEEAEERAD 1913
Cdd:PRK12704 175 IKEIEEEAKEEAD 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
865-1032 |
4.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATER----------------- 927
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraralyrsggsvsy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 928 -----------------------AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEM 984
Cdd:COG3883 105 ldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 826320982 985 AGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQ 1032
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
875-1233 |
4.82e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 875 LEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAED--------EEEINAELTAKKRKLE 946
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitvrlQDLTEKLSEAEDMLAC 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 947 DECSELKK-----DIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAhQQTLDDLQAEEDKVNT 1021
Cdd:TIGR00618 613 EQHALLRKlqpeqDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELL-ASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1022 LTKAKTKLEQQVDDLEGSLEQEKKLRMDLER-------AKRKLEGDLKLAQESTMDIEndkQQLDEKLKKKEFEMSNLQS 1094
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELM---HQARTVLKARTEAHFNNNE 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1095 KIEDEQAVGMQLQKKIKELQARTeeleeeieaerasRAKAEKQRSdLSRELEEISERLEEAGGATSAQIEMNKKREAEFQ 1174
Cdd:TIGR00618 769 EVTAALQTGAELSHLAAEIQFFN-------------RLREEDTHL-LKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFL 834
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1175 KMRRdlEEATLQHEATaaalrkkhadsvAELGEQIDNLQRvKQKLEKEKSELKMEIDDL 1233
Cdd:TIGR00618 835 SRLE--EKSATLGEIT------------HQLLKYEECSKQ-LAQLTQEQAKIIQLSDKL 878
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1386-1921 |
5.05e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.02 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1386 EELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKqrlqNEVEDLMIDVERSNAacialDKKQRNFDKVLAewKHKYEET 1465
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLERAQT-----EEAQAKQDSELA--KLRVEEM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1466 qaELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQ----IAEGGKHIHELEKVKKQIDQEKSE 1541
Cdd:pfam05701 111 --EQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSErdiaIKRAEEAVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1542 LQASLEEAE----ASLEHEEGKIlRIQLELNQVKSEIDRKIAEKDEEIDQLkRNHLRVVESMQSTLDAeirsrNDALRIK 1617
Cdd:pfam05701 189 LIATKESLEsahaAHLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASALLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1618 KKMEgdLNE-MEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQ 1696
Cdd:pfam05701 262 LKAE--LAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAELAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1697 TERSRKMAeqelldaservqllhtqntslintkkklETDISHIQGEMEDIVQEARNAEEKAKKAitdAAMMAEELKKEQD 1776
Cdd:pfam05701 340 LRQREGMA----------------------------SIAVSSLEAELNRTKSEIALVQAKEKEA---REKMVELPKQLQQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1777 TSAHLERMKKNMEQTVKDLQHRLDEAEQlalkgGKKQIQKLEARVRELENEVEG---EQRRNVEAVKSLRKHER------ 1847
Cdd:pfam05701 389 AAQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEAakaSEKLALAAIKALQESESsaestn 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1848 ---RVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNK 1921
Cdd:pfam05701 464 qedSPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1135-1371 |
5.09e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1135 EKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEataaalrKKHADSVAELGEQidNLQR 1214
Cdd:COG5022 834 ETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQEL-------KIDVKSISSLKLV--NLEL 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1215 VKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMcrtledQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLD 1294
Cdd:COG5022 905 ESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNI------DLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLK 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1295 EKEALVSQL------SRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAK--AELQRGMSKA 1366
Cdd:COG5022 979 KSTILVREGnkanseLKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKplQKLKGLLLLE 1058
|
....*
gi 826320982 1367 NSEVA 1371
Cdd:COG5022 1059 NNQLQ 1063
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1671-1912 |
5.57e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1671 EQLAMVERRANLMQAEVEELrasleQTERSRKMAEQELL--DASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQ 1748
Cdd:pfam07888 20 TDMLLVVPRAELLQNRLEEC-----LQERAELLQAQEAAnrQREKEKERYKRDREQWERQRRELESRVAELKEELRQSRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1749 EARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEqLALKGGKKQIQKLEARVRELENEV 1828
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1829 EGEQRRNVEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQsnvnLARFRKIQHELEEA 1908
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNAS 249
|
....
gi 826320982 1909 EERA 1912
Cdd:pfam07888 250 ERKV 253
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
866-1068 |
5.60e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.86 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 866 AKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINA---ELTAKK 942
Cdd:PRK00106 24 IKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSerqELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 943 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEmaglDENIAKLAKEKkalqEAHQQTLDDLQAEEDKVNTL 1022
Cdd:PRK00106 104 SRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELERVAALSQAEAREIIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 826320982 1023 TKAKTKLEQQVDDLEGSLEQEKKLRMD------LERAKRKLEGDLKLAQEST 1068
Cdd:PRK00106 176 AETENKLTHEIATRIREAEREVKDRSDkmakdlLAQAMQRLAGEYVTEQTIT 227
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1466-1937 |
5.78e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1466 QAELEASQKESRSlstelfkvknaYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQAS 1545
Cdd:TIGR00606 230 EAQLESSREIVKS-----------YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1546 LEEAEASLEHEEG--------KILRIQLE----------LNQVKSEIDRKIAEKDEEIDQ-----LKRNHLRVVESMQST 1602
Cdd:TIGR00606 299 TDEQLNDLYHNHQrtvrekerELVDCQREleklnkerrlLNQEKTELLVEQGRLQLQADRhqehiRARDSLIQSLATRLE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1603 LDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANL 1682
Cdd:TIGR00606 379 LDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKF 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1683 MQAEVEELRASLE---QTERSRKMAEQELLDASE---------RVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEA 1750
Cdd:TIGR00606 459 VIKELQQLEGSSDrilELDQELRKAERELSKAEKnsltetlkkEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1751 RNAEEKAKK-------------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLAlKGGKKQIQKL 1817
Cdd:TIGR00606 539 MLTKDKMDKdeqirkiksrhsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNK-NHINNELESK 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1818 EARVRELENEV---------EGEQRRNVEAVKSLRK-----------HERRVKELTYQT-------EEDRKNVLRLQDLV 1870
Cdd:TIGR00606 618 EEQLSSYEDKLfdvcgsqdeESDLERLKEEIEKSSKqramlagatavYSQFITQLTDENqsccpvcQRVFQTEAELQEFI 697
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1871 DKLQTKVKAYKRQAEEAEEQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1937
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1348-1552 |
6.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1348 QYEEEQEAKAELQRGMSKANSEVAQWRTKYEtdaihrteELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEV 1427
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1428 EDLMIDVERSNAACIALDK--KQRNFDKVLAEWK-------------HKYEETQAELEASQKESRSLSTELFKVKNAYEE 1492
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllGSESFSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1493 TLDQLETLKRENknlQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEAS 1552
Cdd:COG3883 169 AKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
865-1323 |
6.59e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQ------LIKTKIQLEA----KIKEATERAEDEEEI 934
Cdd:PRK10246 442 LAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQearikdLEAQRAQLQAgqpcPLCGSTSHPAVEAYQ 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 935 NAELTAKKRKLedecselkkdiDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDL-- 1012
Cdd:PRK10246 522 ALEPGVNQSRL-----------DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLni 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1013 -QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRmDLERAKRKLEGDLKLAQEStmdIENDKQQLDEKLKKKEFEMSN 1091
Cdd:PRK10246 591 tLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIA-AHNQQIIQYQQQIEQRQQQ---LLTALAGYALTLPQEDEEASW 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1092 LQSKiEDEQAVGMQLQKKIKELQARTEELEEEIEAERASRAKAEKQRSDLSRELEEISERleeaggATSAQIEMNKKREA 1171
Cdd:PRK10246 667 LATR-QQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ------CLSLHSQLQTLQQQ 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1172 EFQKMRRdLEEATLQHEATAAALRkkHADSVAELGEQIDNLQRvkQKLEKEKSELKMEIDDLASNMETVSKAkgnFEKMC 1251
Cdd:PRK10246 740 DVLEAQR-LQKAQAQFDTALQASV--FDDQQAFLAALLDEETL--TQLEQLKQNLENQRQQAQTLVTQTAQA---LAQHQ 811
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 1252 RTLEDQLSEVKTKEEEQQRLinELSAQKARLHTES-GEFSRQLDEKEALVSQLsrgkQAFTQQIEELKRQLEE 1323
Cdd:PRK10246 812 QHRPDGLDLTVTVEQIQQEL--AQLAQQLRENTTRqGEIRQQLKQDADNRQQQ----QALMQQIAQATQQVED 878
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1207-1673 |
6.75e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1207 EQIDNLQRVKQKLEKEKSEL----------KMEIDDLASnmETVSKAKGNFEKMC-RTLEDQLSEVKTKEEEQQRLINEL 1275
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLaqapaklrqaQAELEALKD--DNDEETRETLSTLSlRQLESRLAQTLDQLQNAQNDLAEY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1276 SAQKARLHTESgefsrqldekEALVSQLSrgkqAFTQQIEELKRQLEEETKAKNALAHAvqsarhdcdlLREQYEEEQ-- 1353
Cdd:PRK11281 148 NSQLVSLQTQP----------ERAQAALY----ANSQRLQQIRNLLKGGKVGGKALRPS----------QRVLLQAEQal 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1354 -EAKAELQRGMSKANSEVAQWRTKyetdaihRTEELEEAKKKLAQRLQDAEehvEAVNSKCASL-EKTKQRLQNevedlm 1431
Cdd:PRK11281 204 lNAQNDLQRKSLEGNTQLQDLLQK-------QRDYLTARIQRLEHQLQLLQ---EAINSKRLTLsEKTVQEAQS------ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1432 idversnaaciaLDKKQR-NFDKVLA-EWKHKYEETQAELEASQKeSRSLSTELFKVKNayeetldQLETLKRENKNLQQ 1509
Cdd:PRK11281 268 ------------QDEAARiQANPLVAqELEINLQLSQRLLKATEK-LNTLTQQNLRVKN-------WLDRLTQSERNIKE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1510 EISDLTEQIAeggkhiheLEKVkkqIDQEKSELQASLEEAEASleheeGKI--LRI-QLELNQVKSeidrKIAEKDEEID 1586
Cdd:PRK11281 328 QISVLKGSLL--------LSRI---LYQQQQALPSADLIEGLA-----DRIadLRLeQFEINQQRD----ALFQPDAYID 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1587 QLKRNHlrvvesmQSTLDAEIR-SRNDALRIKKKMEGDLN-EMEIQLNHANrqaseairNLRNTQGVLKDTQlhldDAIR 1664
Cdd:PRK11281 388 KLEAGH-------KSEVTDEVRdALLQLLDERRELLDQLNkQLNNQLNLAI--------NLQLNQQQLLSVS----DSLQ 448
|
....*....
gi 826320982 1665 SQddLKEQL 1673
Cdd:PRK11281 449 ST--LTQQI 455
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1143-1482 |
6.90e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1143 RELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKH----------ADSVAELGEQIDNL 1212
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHeeleekykelSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1213 QRVKQKLEKEKSELKmeiDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSR- 1291
Cdd:pfam07888 121 LAQRAAHEARIRELE---EDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEl 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1292 --QLDEKEALVSQLSRGKQAFTQQIEELKR---QLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKA 1366
Cdd:pfam07888 198 rnSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1367 NSEVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAE---EHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERsnaacia 1443
Cdd:pfam07888 278 RLQAAQLTLQLADASLALREGRARWAQERETLQQSAEadkDRIEKLSAELQRLEERLQEERMEREKLEVELGR------- 350
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 826320982 1444 ldkkQRNFDKV-LAEWKHKYEETQAELEASQKESRSLSTE 1482
Cdd:pfam07888 351 ----EKDCNRVqLSESRRELQELKASLRVAQKEKEQLQAE 386
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1549-1779 |
7.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1549 AEASLEHEEGKILRIQLELNQVKSEIDrkiaEKDEEIDQLKRNHLRVVESMQsTLDAEIrsrndalrikKKMEGDLNEME 1628
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELE-ALQAEI----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1629 IQLNHANRQASEAIRNLRNTQGVLKDTQLHLDdaIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQEL 1708
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDVLLG--SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1709 ldaservQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSA 1779
Cdd:COG3883 157 -------AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1297-1409 |
8.12e-04 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 43.46 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1297 EALVSQLSRGKQAFTQQIEELKRQLEEETKAKnALAHAVqSARHDCDLLREQYEEEQEAKAELQRGMSKANSEvaQWRTK 1376
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAI-KLDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS--EDEEE 185
|
90 100 110
....*....|....*....|....*....|...
gi 826320982 1377 YEtDAIHRTEELEEAKKKLAQRLQDAEEHVEAV 1409
Cdd:cd12821 186 LR-RTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1133-1361 |
8.23e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.07 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1133 KAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEatLQHEATAAALRKKHADSVAELGEQidNL 1212
Cdd:pfam06160 183 KLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEH--LNVDKEIQQLEEQLEENLALLENL--EL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1213 QRVKQKLEkeksELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSaQKARLHTESGEFSRQ 1292
Cdd:pfam06160 259 DEAEEALE----EIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQ-QSYTLNENELERVRG 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 826320982 1293 LDEK--------EALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSarhdcdlLREQYEEEQEAKAELQR 1361
Cdd:pfam06160 334 LEKQleelekryDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKES-------LQSLRKDELEAREKLDE 403
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1220-1372 |
8.46e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1220 EKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEAL 1299
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 1300 VSQLSRGKQAFTQQIEELKRQLEeetkaknalahAVQSArhdcdlLREQYEEEQEAKAELQRGMSKANSEVAQ 1372
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLA-----------ALEAA------LDASEKRDRESQAKIADLGRRLNVALAQ 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1740-1933 |
9.98e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1740 QGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlALKGGKKQIQKLEA 1819
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1820 RVRELENEVEGEQRRN-----------VEAVKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAE 1888
Cdd:COG4942 105 ELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 826320982 1889 EQSNVNLARFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1933
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
837-1058 |
1.08e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 837 KIKPLLKSAETEKEMANMKEEFEKAKEELAKSEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQ 916
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 917 LEAKIKEATERAEDEEEInAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATEN-KVKNLTEEmagLDENIAKLA 995
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREALA-ELNDERRERLAEKReRKRELEAE---FDEARIEEA 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 996 KEKKALQEAHQQTLDdlqaeeDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1058
Cdd:PRK02224 652 REDKERAEEYLEQVE------EKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1234-1544 |
1.08e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1234 ASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLIN---ELSAQKARlhtesgefSRQL-DEKEALVSQLSRGKQA 1309
Cdd:COG3096 271 ADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEmarELEELSAR--------ESDLeQDYQAASDHLNLVQTA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1310 FTQQ---------IEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMskansEVAQWRTKYETD 1380
Cdd:COG3096 343 LRQQekieryqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL-----DVQQTRAIQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1381 AIHRTEELEE-------AKKKLAQRLQDAEEHVEAVNSKCASLEktkQRL--------QNE-----VEDLMIDVERSNAA 1440
Cdd:COG3096 418 AVQALEKARAlcglpdlTPENAEDYLAAFRAKEQQATEEVLELE---QKLsvadaarrQFEkayelVCKIAGEVERSQAW 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1441 CIA--LDKKQRNFdKVLAEWKHKYEETQAELE---ASQKESRSLSTELFKVKNAYEETLDQLETLKREnknLQQEISDLT 1515
Cdd:COG3096 495 QTAreLLRRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE---LEAQLEELE 570
|
330 340
....*....|....*....|....*....
gi 826320982 1516 EQIAEGGKHIHELEKVKKQIDQEKSELQA 1544
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1147-1396 |
1.11e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1147 EISERLEEAggatsAQIEMNKKR-EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIdnlqRVKQKLEKEKSE 1225
Cdd:PRK05035 437 EIRAIEQEK-----KKAEEAKARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARV----KAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1226 LKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQ-LS 1304
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAaIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1305 RGK-----QAFTQQIEELKRQLEEETKAKNALAHAVQSARHDC-DLLREQYEEEQEAKAELQRGMSKANSEVAQwrtkYE 1378
Cdd:PRK05035 588 RAKakkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEqQANAEPEEPVDPRKAAVAAAIARAKARKAA----QQ 663
|
250
....*....|....*...
gi 826320982 1379 TDAIHRTEELEEAKKKLA 1396
Cdd:PRK05035 664 QANAEPEEAEDPKKAAVA 681
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1192-1339 |
1.13e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1192 AALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKgnfekmcRTLEDQLSEVKTkEEEQQRL 1271
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-------KKYEEQLGNVRN-NKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1272 INELSAQKAR---LHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSAR 1339
Cdd:COG1579 95 QKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
890-1101 |
1.23e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 890 QLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAeltakkRKLEDECSELKKDIDDLELTLAKVEKE 969
Cdd:PLN03229 536 KLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 970 KHATENKVKNLTEEMaGLDENIAKlakeKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKklrmd 1049
Cdd:PLN03229 610 KKEIELELAGVLKSM-GLEVIGVT----KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK----- 679
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 826320982 1050 LERAKRKLEGDLKLAQEstmdIENDKQQLDEKLKKKeFEMSNLQSKIEDEQA 1101
Cdd:PLN03229 680 LEVAKASKTPDVTEKEK----IEALEQQIKQKIAEA-LNSSELKEKFEELEA 726
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
863-1086 |
1.25e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.99 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 863 EELAKSEAKRKELEEKMVTLMQEK--NDLQLQVQAEADSLADaeercdqliktkiQLEAKIKEATERAEDEEEINAELTA 940
Cdd:pfam18971 617 KDLEKSLRKREHLEKEVEKKLESKsgNKNKMEAKAQANSQKD-------------EIFALINKEANRDARAIAYTQNLKG 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 941 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAkLAKEKKALQEAHQQTLDDLQAEEDK-V 1019
Cdd:pfam18971 684 IKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLG-INPEWISKVENLNAALNEFKNGKNKdF 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1020 NTLTKAKTKLEQQVDDLEGSLEQEKKL-RMDLERAKRKLEGDLKLAQESTMDIEN-DKQQLDEKLKKKE 1086
Cdd:pfam18971 763 SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQKNE 831
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1013-1243 |
1.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1013 QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQ-EKKLrmdlERAKRK-----LEGDLKLAQESTMDIENDKQQLDEKLKKKE 1086
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAAL----EEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1087 FEMSNLQSKIEDEQAVG----------------MQLQKKIKELQARTEELEEEIEAERASRAKAEKQrsdLSRELEEISE 1150
Cdd:COG3206 240 ARLAALRAQLGSGPDALpellqspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1151 RLEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaELGEQIDNLQRVKQKLEKEKSELKMEI 1230
Cdd:COG3206 317 SLE-------AELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLAE 381
|
250
....*....|...
gi 826320982 1231 DDLASNMETVSKA 1243
Cdd:COG3206 382 ALTVGNVRVIDPA 394
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1678-1900 |
1.27e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1678 RRANLMQAEVEELrasLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIvqearnaEEKA 1757
Cdd:COG1842 5 RLSDIIRANINAL---LDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW-------EEKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1758 KKAitdaammaeeLKKEQDTSAH--LERmKKNMEQTVKDLQHRLDEAEQLALKgGKKQIQKLEARVRELENEvegeqRRN 1835
Cdd:COG1842 75 RLA----------LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEK-LKEALRQLESKLEELKAK-----KDT 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1836 VEAVKSLRKHERRVKEL--TYQTEEDRKNVLRLQDLVDKLQTKVKAYK---------RQAEEAEEQSNVN--LARFRK 1900
Cdd:COG1842 138 LKARAKAAKAQEKVNEAlsGIDSDDATSALERMEEKIEEMEARAEAAAelaagdsldDELAELEADSEVEdeLAALKA 215
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
931-1323 |
1.37e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 931 EEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQEAHQQT 1008
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1009 LDDLQAEEdkvntltkaktkLEQQVDDLEGSLEQEKK-----------LRMDLERAKRKLEGDLKLAQEstmdIENdkqQ 1077
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ----IRN---L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1078 LDEKLKKKEFEMSNLQSKIEDEQA-VGMQLQKKIKELQARTEELEEeieaerasrakAEKQRSDLSrelEEISeRLEEAg 1156
Cdd:PRK11281 179 LKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQDL-----------LQKQRDYLT---ARIQ-RLEHQ- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1157 gATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI------------DNLqRVKQKLekeks 1224
Cdd:PRK11281 243 -LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVKNWL----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1225 elkmeidDLASNMEtvskakgnfekmcRTLEDQ---------LSEVKTKEEE---QQRLINELSAQKARLHTESGEFSRQ 1292
Cdd:PRK11281 316 -------DRLTQSE-------------RNIKEQisvlkgsllLSRILYQQQQalpSADLIEGLADRIADLRLEQFEINQQ 375
|
410 420 430
....*....|....*....|....*....|....*
gi 826320982 1293 LDE---KEALVSQLSRG-KQAFTqqiEELKRQLEE 1323
Cdd:PRK11281 376 RDAlfqPDAYIDKLEAGhKSEVT---DEVRDALLQ 407
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1483-1912 |
1.38e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1483 LFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHEL----EKVKKQIDQEKSELQASLEEAEASLEHEEG 1558
Cdd:PRK04778 100 FRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLkdlyRELRKSLLANRFSFGPALDELEKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1559 KILRIQlELNQVKSEID-RKIAEK-DEEIDQLkRNHLRVVESMQSTLDAEIRSRNDALRI---KKKMEG-DLNEMEI--- 1629
Cdd:PRK04778 180 EFSQFV-ELTESGDYVEaREILDQlEEELAAL-EQIMEEIPELLKELQTELPDQLQELKAgyrELVEEGyHLDHLDIeke 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1630 --QLNHANRQASEAIrnlrntqgvlkdTQLHLDDAIRSQDDLKEQL-AMVErranLMQAEVE----------ELRASLEQ 1696
Cdd:PRK04778 258 iqDLKEQIDENLALL------------EELDLDEAEEKNEEIQERIdQLYD----ILEREVKarkyveknsdTLPDFLEH 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1697 TERSRKMAEQELldasERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEArnaeEKAKKAITDAAMMAEELKKeqd 1776
Cdd:PRK04778 322 AKEQNKELKEEI----DRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERI----AEQEIAYSELQEELEEILK--- 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1777 tsaHLERMKKNMEQTVKDLQhRLDEAEQLALKGGKKQIQKLEARVRELEnevegeqRRNV----EAVKSLRKH-ERRVKE 1851
Cdd:PRK04778 391 ---QLEEIEKEQEKLSEMLQ-GLRKDELEAREKLERYRNKLHEIKRYLE-------KSNLpglpEDYLEMFFEvSDEIEA 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 826320982 1852 LTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEqsNVNLA--------RFRKIQHELEEAEERA 1912
Cdd:PRK04778 460 LAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVE--NATLTeqliqyanRYRSDNEEVAEALNEA 526
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
885-1103 |
1.40e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 885 EKNDLQLQVQAEADSLADAEERCDQL---IKTKIQLEAKIKEA------TERA---EDEEEINAELTAKKRKLE--DECS 950
Cdd:NF012221 1557 AQNALADKERAEADRQRLEQEKQQQLaaiSGSQSQLESTDQNAletngqAQRDailEESRAVTKELTTLAQGLDalDSQA 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 951 ELKKDIDD------LELTLAKVEKEKHATENKVKNLTEEMAglDENIAKLAKEKKALQ--EAHQQTLDDLQAEEDKvnTL 1022
Cdd:NF012221 1637 TYAGESGDqwrnpfAGGLLDRVQEQLDDAKKISGKQLADAK--QRHVDNQQKVKDAVAksEAGVAQGEQNQANAEQ--DI 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1023 TKAKTKLEQQVDDL---EGSLEQ-EKKLRMDLERAKRKLEGDLKLAQESTMDIEND----KQQLDEKLKKKEFEMSNLQS 1094
Cdd:NF012221 1713 DDAKADAEKRKDDAlakQNEAQQaESDANAAANDAQSRGEQDASAAENKANQAQADakgaKQDESDKPNRQGAAGSGLSG 1792
|
....*....
gi 826320982 1095 KIEDEQAVG 1103
Cdd:NF012221 1793 KAYSVEGVA 1801
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
988-1099 |
1.80e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 42.92 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 988 DENIAKLAKEKKA-------LQEAHQQTLDDLQAEEDKVNT--------LTKAKTKLEQQVDDLEGSLEQEKKLRMDLER 1052
Cdd:pfam03148 207 QDNIERAEKERAAsaqlrelIDSILEQTANDLRAQADAVNFalrkrieeTEDAKNKLEWQLKKTLQEIAELEKNIEALEK 286
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1053 AKRKLEGDLKLAQ------------ESTMD------------IENDKQQLDEKLKKKEFEMSNL---QSKIEDE 1099
Cdd:pfam03148 287 AIRDKEAPLKLAQtrlenrtyrpnvELCRDeaqyglvdevkeLEETIEALKQKLAEAEASLQALertRLRLEED 360
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
865-1197 |
2.07e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKELEEKMVTLMQEkndLQLQVQAEADSLADAEErcdqliktkiQLEAKIKEATERAEDEEEINAE---LTAK 941
Cdd:PRK04778 131 LLESEEKNREEVEQLKDLYRE---LRKSLLANRFSFGPALD----------ELEKQLENLEEEFSQFVELTESgdyVEAR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 942 K--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----LTEEMAGLDENiaKLAKEKKALQEAHQQTLDDLqaE 1015
Cdd:PRK04778 198 EilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEGYHLDHL--DIEKEIQDLKEQIDENLALL--E 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1016 EDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKlkkkeFEMSnlqsk 1095
Cdd:PRK04778 274 ELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQS-----YTLN----- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1096 iEDEQAVGMQLQKKIKELQARTEELEEEIeaerasrAKAEKQRSDLSRELEEISERLEEAggatsaqiemnKKREAEFQK 1175
Cdd:PRK04778 344 -ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYSELQEELEEILKQLEEI-----------EKEQEKLSE 404
|
330 340
....*....|....*....|..
gi 826320982 1176 MRRDLEEATLQHEATAAALRKK 1197
Cdd:PRK04778 405 MLQGLRKDELEAREKLERYRNK 426
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
900-1153 |
2.17e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 900 LADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDdlELTLAKVEkekhaTENKVKN 979
Cdd:pfam00038 56 IEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLD--EATLARVD-----LEAKIES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 980 LTEEMAGLDENiakLAKEKKALQEAHQQTldDLQAEEDKVNT--LTKAKTKLEQQVDdlegslEQEKKLRMDLERA-KRK 1056
Cdd:pfam00038 129 LKEELAFLKKN---HEEEVRELQAQVSDT--QVNVEMDAARKldLTSALAEIRAQYE------EIAAKNREEAEEWyQSK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1057 LEGDLKLAQESTMDIENDKQQLDE---KLKKKEFEMSNLQSKIEdeqavgmQLQKKIKELQARTEeleeeieaerASRAK 1133
Cdd:pfam00038 198 LEELQQAAARNGDALRSAKEEITElrrTIQSLEIELQSLKKQKA-------SLERQLAETEERYE----------LQLAD 260
|
250 260
....*....|....*....|
gi 826320982 1134 AEKQRSDLSRELEEISERLE 1153
Cdd:pfam00038 261 YQELISELEAELQETRQEMA 280
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1479-1714 |
2.24e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1479 LSTELFKVKNAYE---ETLDQLETLKRENKNLQQEISDLTEQIAeggkhihELEKVK------KQIDQEKS------ELQ 1543
Cdd:COG0497 153 LEELLEEYREAYRawrALKKELEELRADEAERARELDLLRFQLE-------ELEAAAlqpgeeEELEEERRrlsnaeKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1544 ASLEEAEASLEHEEGKILRIqleLNQVKSEIDRkIAEKDEEIDQLkrnhLRVVESMQSTLD---AEIRSRNDALrikkkm 1620
Cdd:COG0497 226 EALQEALEALSGGEGGALDL---LGQALRALER-LAEYDPSLAEL----AERLESALIELEeaaSELRRYLDSL------ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1621 EGD---LNEMEIQLNhanrqaseAIRNLRNTQGVLkdtqlhLDDAIRSQDDLKEQLAMVERRanlmQAEVEELRASLEQt 1697
Cdd:COG0497 292 EFDperLEEVEERLA--------LLRRLARKYGVT------VEELLAYAEELRAELAELENS----DERLEELEAELAE- 352
|
250
....*....|....*..
gi 826320982 1698 ersrkmAEQELLDASER 1714
Cdd:COG0497 353 ------AEAELLEAAEK 363
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1204-1529 |
2.27e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1204 ELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLH 1283
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1284 TESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELK-------RQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAK 1356
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELERMKerakkagAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1357 AELQRGMSKANSEVAQWRTKYETdAIHRTEELEEAKKKLA---QRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMID 1433
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1434 VERSNaacIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTELFKVKNAYEE------------------TLD 1495
Cdd:pfam07888 281 AAQLT---LQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermereklevelgrekdcNRV 357
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 826320982 1496 QLETLKRENKNL-------QQEISDLTEQIAEGGKHIHELE 1529
Cdd:pfam07888 358 QLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLE 398
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1526-1698 |
2.29e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1526 HELEKVKK-----QIDQekSELQASLEEAEASLEHEEGKILRIQLELNQ---VKSEIDRKIAEKDEEIDQLKRnhlrvve 1597
Cdd:pfam00529 37 KEGDRVKAgdvlfQLDP--TDYQAALDSAEAQLAKAQAQVARLQAELDRlqaLESELAISRQDYDGATAQLRA------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1598 smqstLDAEIRSRNDALrikKKMEGDLNEMEIQLNH---ANRQASEAIRNLRNTQGVLKDTQLHLD----DAIRSQddlK 1670
Cdd:pfam00529 108 -----AQAAVKAAQAQL---AQAQIDLARRRVLAPIggiSRESLVTAGALVAQAQANLLATVAQLDqiyvQITQSA---A 176
|
170 180
....*....|....*....|....*...
gi 826320982 1671 EQLAMVERRANLMQAEVEELRASLEQTE 1698
Cdd:pfam00529 177 ENQAEVRSELSGAQLQIAEAEAELKLAK 204
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1227-1699 |
2.49e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1227 KMEIDDLASNMETVskakgnfEKMCRTLEDQLSEVKTKEEEQQRLINELSAQ----KARLHTESGEFSRQLDEKEalvsq 1302
Cdd:PRK04778 104 KHEINEIESLLDLI-------EEDIEQILEELQELLESEEKNREEVEQLKDLyrelRKSLLANRFSFGPALDELE----- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1303 lsrgkqaftQQIEELKRQLEEETKAKNALAHaVQSarhdcdllREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETdai 1382
Cdd:PRK04778 172 ---------KQLENLEEEFSQFVELTESGDY-VEA--------REILDQLEEELAALEQIMEEIPELLKELQTELPD--- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1383 hRTEELEEAkkklAQRLQDAEEHVEAVNskcasLEKTKQRLQNEVEDLMIDVERsnaacIALDKKQRNFDKVLAEWKHKY 1462
Cdd:PRK04778 231 -QLQELKAG----YRELVEEGYHLDHLD-----IEKEIQDLKEQIDENLALLEE-----LDLDEAEEKNEEIQERIDQLY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1463 EETQAELEASQKesrslstelfkVKNAYEETLDQLETLKRENKNLQQEISDLTE--QIAEggkhiHELEKVKkQIDQEKS 1540
Cdd:PRK04778 296 DILEREVKARKY-----------VEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNE-----SELESVR-QLEKQLE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1541 ELQASLEEAEASLEHEEgkilriqlelnQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKM 1620
Cdd:PRK04778 359 SLEKQYDEITERIAEQE-----------IAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1621 EG-------------------DLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERran 1681
Cdd:PRK04778 428 HEikryleksnlpglpedyleMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ--- 504
|
490 500
....*....|....*....|....
gi 826320982 1682 LMQ------AEVEELRASLEQTER 1699
Cdd:PRK04778 505 LIQyanryrSDNEEVAEALNEAER 528
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1257-1869 |
2.68e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1257 QLSEVKTKEEEQQRLINELSA----QKARLHTESGEFSRQLDEKE-------------ALVSQLSRGKQ---AFTQQIEE 1316
Cdd:PRK10246 312 QIEEVNTRLQSTMALRARIRHhaakQSAELQAQQQSLNTWLAEHDrfrqwnnelagwrAQFSQQTSDREqlrQWQQQLTH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1317 LKRQLE-----------EETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQwrtkyetdaihRT 1385
Cdd:PRK10246 392 AEQKLNalpaitltltaDEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQ-----------RN 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1386 EELEEAKkklaQRLQDAEEHVEAVNSKC------ASLEKTKQRLQnevedlmidverSNAACialdkkqrnfdKVLAEWK 1459
Cdd:PRK10246 461 AALNEMR----QRYKEKTQQLADVKTICeqeariKDLEAQRAQLQ------------AGQPC-----------PLCGSTS 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1460 HKYEETQAELEASQKESRslstelfkvknayeetLDQLEtlkrenknlqQEISDLTEqiaEGGKHIHELEKVKKQIDQEK 1539
Cdd:PRK10246 514 HPAVEAYQALEPGVNQSR----------------LDALE----------KEVKKLGE---EGAALRGQLDALTKQLQRDE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1540 SELQASLEEAEASLEHEEGKILRIQLELnQVKSEIDRKIAEKDE---EIDQLKRNHlrvvesmqstldaeirsrndalri 1616
Cdd:PRK10246 565 SEAQSLRQEEQALTQQWQAVCASLNITL-QPQDDIQPWLDAQEEherQLRLLSQRH------------------------ 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1617 kkkmegdlnEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQ 1696
Cdd:PRK10246 620 ---------ELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNR 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1697 TERSRKM-----AEQELLDASERVQL-----LHTQNTSLINTKKKLETDISHIQGEMEDiVQEARNAEEKAKKAITDAAM 1766
Cdd:PRK10246 691 IQQLTPLletlpQSDDLPHSEETVALdnwrqVHEQCLSLHSQLQTLQQQDVLEAQRLQK-AQAQFDTALQASVFDDQQAF 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1767 MAEELKKEqdTSAHLERMKKNMEQtvkdlqhRLDEAEQLALKGGKKQIQKLEARVRELENEVEGEQRRNVEAV--KSLRK 1844
Cdd:PRK10246 770 LAALLDEE--TLTQLEQLKQNLEN-------QRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRE 840
|
650 660
....*....|....*....|....*
gi 826320982 1845 HERRVKELTYQTEEDRKNVLRLQDL 1869
Cdd:PRK10246 841 NTTRQGEIRQQLKQDADNRQQQQAL 865
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1704-1890 |
2.87e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1704 AEQELLDASERVQLLHTQNTSLINTKKKLETDIShiqgEMEDIVQEARNAEEKAKKAITDAAMMAEELKKE-QDTSAHLE 1782
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELA----ELEDELAALEARLEAAKTELEDLEKEIKRLELEiEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1783 RMKKNMEQ--TVKDLQHRLDEAEQLalkggKKQIQKLEARVRELENEVEgeqrrnvEAVKSLRKHERRVKELTYQTEEDR 1860
Cdd:COG1579 77 KYEEQLGNvrNNKEYEALQKEIESL-----KRRISDLEDEILELMERIE-------ELEEELAELEAELAELEAELEEKK 144
|
170 180 190
....*....|....*....|....*....|
gi 826320982 1861 KnvlRLQDLVDKLQTKVKAYKRQAEEAEEQ 1890
Cdd:COG1579 145 A---ELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1573-1923 |
2.88e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1573 EIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVL 1652
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1653 KDTQLHLDDAIRSQDDLKEQLAMVERRANLMQAEVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKL 1732
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1733 ETDIShiQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKK 1812
Cdd:COG4372 163 QEELA--ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1813 QIQKLEARVRELENEVEGEQRRNVEA-VKSLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQS 1891
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAiLVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350
....*....|....*....|....*....|..
gi 826320982 1892 NVNLARFRKIQHELEEAEERADIAESQVNKLR 1923
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1313-1522 |
3.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1313 QIEELKRQLEEETKAKNALAHAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQwrtkyetdaihRTEELEEAK 1392
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-----------AEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1393 KKLAQRLQDAEEHVEAVN---------------SKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAE 1457
Cdd:COG3883 86 EELGERARALYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 826320982 1458 wkhkYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEQIAEGG 1522
Cdd:COG3883 166 ----LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
994-1405 |
3.47e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 994 LAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlkLAQESTMDIEN 1073
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1074 DKQQLDEKLKKKEFEMSNLQSKIEDEQAVG---MQLQKKIKELQARTEELEEEIEAERASRAKAEkQRSDLSRELEEISE 1150
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAeeaQALKDEMDILRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1151 R----------LEEA---GGATSAQIEMNKKREAEFQKMrrdLEEATLQHEATAAALRKKHadsvaelgEQIDNLQRVKQ 1217
Cdd:pfam05622 160 RnaeymqrtlqLEEElkkANALRGQLETYKRQVQELHGK---LSEESKKADKLEFEYKKLE--------EKLEALQKEKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1218 KLEKEKSELKMEIDDL---ASNMETVSKAKGNFEKMCRTLEDQLSEVKTKE--EEQQRLINE----LSAQKARLHTESGE 1288
Cdd:pfam05622 229 RLIIERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEirEKLIRLQHEnkmlRLGQEGSYRERLTE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1289 FSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNalahAVQSARHDCDLLREQYEEEQEAKAELQRGMSKANS 1368
Cdd:pfam05622 309 LQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQ----EQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKE 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 826320982 1369 EVAQWRTKYETDAIHRTEELEEAKKKLAQRLQDAEEH 1405
Cdd:pfam05622 385 QIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEER 421
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
805-1910 |
3.48e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 805 KMMERRESIFCIQYNIRAfMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKeefekaKEELAKSEAKRKELEEKMVTLMQ 884
Cdd:PTZ00440 317 KIEKGKEYIKRIQNNNIP-PQVKKDELKKKYFESAKHYASFKFSLEMLSML------DSLLIKKEKILNNLFNKLFGDLK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 885 EKndlqlqvqaeADSLADAEercdQLIKTKIQLEAKIKEATERAEDEEEINAELTAK-KRKLEDECSELKKDIDDLELTL 963
Cdd:PTZ00440 390 EK----------IETLLDSE----YFISKYTNIISLSEHTLKAAEDVLKENSQKIADyALYSNLEIIEIKKKYDEKINEL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 964 AKvekekhaTENKVKNLTEEMAGLdeniAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQE 1043
Cdd:PTZ00440 456 KK-------SINQLKTLISIMKSF----YDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNI 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1044 KKLRMDLERAKRKLEGDLKLaqestmdIENDKQQLdEKLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEE 1123
Cdd:PTZ00440 525 EDYYITIEGLKNEIEGLIEL-------IKYYLQSI-ETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNI 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1124 IEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqieMNKKREAEFQKMRRDLEEATLQHEATAaalrkKHADSVA 1203
Cdd:PTZ00440 597 IQQIEELINEALFNKEKFINEKNDLQEKVKYI---------LNKFYKGDLQELLDELSHFLDDHKYLY-----HEAKSKE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1204 ELGEQIDNLQRVKQKLEKEKSE--------LKMEIDDLASNMETVSKAkgNFEKMCRTLEDQLSEVKTKEEEQQRLINEL 1275
Cdd:PTZ00440 663 DLQTLLNTSKNEYEKLEFMKSDnidniiknLKKELQNLLSLKENIIKK--QLNNIEQDISNSLNQYTIKYNDLKSSIEEY 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1276 SAQKARLHTesgeFSRQLDE-KEALVSQL-------SRGKQAFTQQIEELKRQLEEETKAKNALAHAVQSARHDCDLLre 1347
Cdd:PTZ00440 741 KEEEEKLEV----YKHQIINrKNEFILHLyendkdlPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLL-- 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1348 QYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIHRTE---ELEEAKKKLAQRLQDAEEHVEAVNS------------- 1411
Cdd:PTZ00440 815 NSYNILIQKLEAHTEKNDEELKQLLQKFPTEDENLNLKElekEFNENNQIVDNIIKDIENMNKNINIiktlniainrsns 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1412 ---KCASLEKTKQRLQNEVEDLMIDVERSNaacIALDKKQRNFDKVLAEWKHKYEETQAELEASQkesrsLSTELFKVKN 1488
Cdd:PTZ00440 895 nkqLVEHLLNNKIDLKNKLEQHMKIINTDN---IIQKNEKLNLLNNLNKEKEKIEKQLSDTKINN-----LKMQIEKTLE 966
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1489 AYEET-----------LDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELekvkkqIDQEKSELQASLEEAEASLEHE- 1556
Cdd:PTZ00440 967 YYDKSkeningndgthLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDL------IKKQHDDIIELIDKLIKEKGKEi 1040
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1557 EGKILRIQLELNQVKSEIDRKIAEKDEEIDQ--LKRNHLRVVESMQSTLDAEIRSRNDAL-RIKKKMEGDL----NEMEI 1629
Cdd:PTZ00440 1041 EEKVDQYISLLEKMKTKLSSFHFNIDIKKYKnpKIKEEIKLLEEKVEALLKKIDENKNKLiEIKNKSHEHVvnadKEKNK 1120
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1630 QLNHANRQaseairnlrntQGVLKDTQLHLDDAIRSQDDLKEQLAMVErranlmqaEVEELRasleqtersrkmAEQELL 1709
Cdd:PTZ00440 1121 QTEHYNKK-----------KKSLEKIYKQMEKTLKELENMNLEDITLN--------EVNEIE------------IEYERI 1169
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1710 DASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM 1788
Cdd:PTZ00440 1170 LIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDhLTTFEYNAYYDKATASYENIEELTTEAKGLKGEANR 1249
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1789 EQTVKDLQhRLDEAEQLALKGGKKQIQKLEARVRELENEVEGEQRRNVEAV-KSLRKHERRVKELTYQTEEDRKNVLRLQ 1867
Cdd:PTZ00440 1250 STNVDELK-EIKLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKIlKEILNSTKKAEEFSNDAKKELEKTDNLI 1328
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*
gi 826320982 1868 DLVDKLQTKVKAYKRQAEEAEE--QSNVNLARFRKIQHELEEAEE 1910
Cdd:PTZ00440 1329 KQVEAKIEQAKEHKNKIYGSLEdkQIDDEIKKIEQIKEEISNKRK 1373
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1106-1798 |
3.51e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1106 LQKKIKELQaRTEELEEEIEAERASR--AKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKM------- 1176
Cdd:pfam10174 1 LQAQLRDLQ-RENELLRRELDIKESKlgSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLqltiqal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1177 ------RRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNFEKM 1250
Cdd:pfam10174 80 qdelraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1251 CRTLEDQL---SEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQ---------AFTQQIEELK 1318
Cdd:pfam10174 160 IKKLLEMLqskGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQlqpdpaktkALQTVIEMKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1319 RQLEEETKAKNALAHAVQSARHDCDLLREQYEEE--------------QEAKAELQRGMSKANSEVAQWRTKYETdaihr 1384
Cdd:pfam10174 240 TKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEikqmevykshskfmKNKIDQLKQELSKKESELLALQTKLET----- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1385 teeleeakkkLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAaciALDKKQRnfdkvlaewkhkyee 1464
Cdd:pfam10174 315 ----------LTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKES---FLNKKTK--------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1465 tqaELEASQKESRSLSTELFKVKnayeetlDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQIDQEKSELQA 1544
Cdd:pfam10174 367 ---QLQDLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDT 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1545 SLEEAEASLEHEEGKILRIqlelnqvKSEIDRKIAEKDEEIDQLKR---------NHLR--VVESMQSTLDAEIRSRNDA 1613
Cdd:pfam10174 437 ALTTLEEALSEKERIIERL-------KEQREREDRERLEELESLKKenkdlkekvSALQpeLTEKESSLIDLKEHASSLA 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1614 LRIKKKmEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDAIRSQdDLKEQLAMVERRANLMQAEVEELRAS 1693
Cdd:pfam10174 510 SSGLKK-DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIR-LLEQEVARYKEESGKAQAEVERLLGI 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1694 LEQTERSRKMAEQELLDASERVQLLH-TQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELK 1772
Cdd:pfam10174 588 LREVENEKNDKDKKIAELESLTLRQMkEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKT 667
|
730 740
....*....|....*....|....*.
gi 826320982 1773 KEQdtsahLERMKKNMEQTVKDLQHR 1798
Cdd:pfam10174 668 RQE-----LDATKARLSSTQQSLAEK 688
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
911-1182 |
3.61e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 911 IKTKIQLEAKIKEATERAEDEEEINAELTAKKRKLEDECSELKKDID--------------DLELTLAKVEKEKHATENK 976
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaaiyaeqermamERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 977 vKNLTEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQA-------EEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKlRMD 1049
Cdd:pfam17380 364 -RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAarkvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVR-RLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1050 LERAkRKLEGDLKLAQESTMDIENDKQQLDEKlKKKEFEMsnlqSKIEDEQAVGMQLQKKI--KELQARteeleeeieae 1127
Cdd:pfam17380 442 EERA-REMERVRLEEQERQQQVERLRQQEEER-KRKKLEL----EKEKRDRKRAEEQRRKIleKELEER----------- 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 826320982 1128 RASRAKAEKQRSDLSRELEEIS------ERLEEAGGATSAQIEMNKKREAEfQKMRRDLEE 1182
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQkaiyeeERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1404-1710 |
3.61e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1404 EHVEAVNSKCAS--LEKTKQ-RLQNEVEDLMIDVERSNAACIALDKKQRNFDK---VLAEWKHKYEETQAELEASQKESR 1477
Cdd:pfam17380 279 QHQKAVSERQQQekFEKMEQeRLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1478 slstelfkvknayeetldqletlKRENKNLQQEisdlteQIAEGGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEE 1557
Cdd:pfam17380 359 -----------------------KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1558 gkilriqlelnqvksEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEiRSRndalrikkkmegdlnEME-IQLNHANR 1636
Cdd:pfam17380 410 ---------------ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE-RAR---------------EMErVRLEEQER 458
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 826320982 1637 QasEAIRNLRNTQGVLKDTQLHLDDAIRSQDDLKEQlamverRANLMQAEVEELRASLEQTERSRKMAEQELLD 1710
Cdd:pfam17380 459 Q--QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| zf-C4H2 |
pfam10146 |
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ... |
1474-1603 |
3.67e-03 |
|
Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumour-associated antigen HCA127 in humans but this could not confirmed.
Pssm-ID: 462963 [Multi-domain] Cd Length: 213 Bit Score: 40.82 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1474 KESRSLSTELFKVKNayeETLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELekvkKQIDQEKSELQASLEEAEASL 1553
Cdd:pfam10146 3 KDIRHKTAQLEKLKE---RLLKELEAHENEEKCLKEYKKEMELLLQEKMAHVEEL----RLIHADINKMEKVIKEAEEER 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 826320982 1554 EHEEGKILRIQLELNQVKSEIDRKIaEKDEEIDQLKRNHLRVVESMQSTL 1603
Cdd:pfam10146 76 NRVLEGAVRLHEEYIPLKLEIDRMR-RELLGLEELPLLHEEEEDLIQTTI 124
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1453-1657 |
3.67e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1453 KVLAEWKHKYEETQAEL--EASQKESRSLSTELFKVKNAYEETLDQLETLKRENK--NLQQEISDLTEQIAEggkhiheL 1528
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------L 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1529 EKVKKQIDQEKSELQASLEEAEASLEHEEG----------------KILRIQLELNQVKS----------EIDRKIAEKD 1582
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDalpellqspviqqlraQLAELEAELAELSArytpnhpdviALRAQIAALR 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 826320982 1583 EEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQL 1657
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1374-1509 |
3.68e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 42.31 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1374 RTKYETDAIHRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQrnfdK 1453
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 1454 VLAEWKHKYEETQAELEASQKESRSLSTELFKVknayeetLDQLETLKRENKNLQQ 1509
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQV-------LDKVQEIHEDCSVLLQ 133
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
904-1045 |
3.81e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 904 EERCDQLIKTKIQLEakiKEATERAEDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 982
Cdd:smart00787 136 EWRMKLLEGLKEGLD---ENLEGLKEDYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 826320982 983 EMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKK 1045
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
884-1068 |
3.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 884 QEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAedeEEINAELTAKKRKLEDECSELKKDI------- 956
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERAralyrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 957 ------------DDLELTLAKVEKEKHATENKvknlTEEMAGLDENIAKLAKEKKALQEAhQQTLDDLQAE-EDKVNTLT 1023
Cdd:COG3883 100 gsvsyldvllgsESFSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAK-LAELEALKAElEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 826320982 1024 KAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEST 1068
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1414-1820 |
4.10e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1414 ASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELeASQKESRSLSTELFKvknayeet 1493
Cdd:pfam15964 321 SSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKEL-ASQQEKRAQEKEALR-------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1494 ldqlETLKRENKNLQQEISDLTEQIAEggkhiheLEKVKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSE 1573
Cdd:pfam15964 392 ----KEMKKEREELGATMLALSQNVAQ-------LEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQ 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1574 IDRKIAEKDEEIDQLKRNHLRVVEsmqsTLDAEIrsrndalrikKKMEGDLNEMEIQLNHANRQASEAIRN-LRNTQGVL 1652
Cdd:pfam15964 461 TKMKKDEAEKEHREYRTKTGRQLE----IKDQEI----------EKLGLELSESKQRLEQAQQDAARAREEcLKLTELLG 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1653 K-DTQLHLddaIRSQDDLKEQLAMVERRANLMQAEVEElrasLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTK-- 1729
Cdd:pfam15964 527 EsEHQLHL---TRLEKESIQQSFSNEAKAQALQAQQRE----QELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKee 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1730 -----KKLETDISHIQGEMEDIVQEARNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQ 1804
Cdd:pfam15964 600 cctlaKKLEEITQKSRSEVEQLSQEKEYLQDRLEK-------LQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQ 672
|
410
....*....|....*.
gi 826320982 1805 LALKGGKKQIQKLEAR 1820
Cdd:pfam15964 673 QLVQLLSKQNQLFKER 688
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1166-1336 |
4.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1166 NKKREAEFQKmrrdlEEATLqhEATAAALRKKhADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKG 1245
Cdd:PRK12704 46 EAKKEAEAIK-----KEALL--EAKEEIHKLR-NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1246 NFEKMCRTLEDQLSEVKTKEEEQ-QRL--INELSAQKARlhtesgefSRQLDEkeaLVSQLSRGKQAFTQQIEElKRQLE 1322
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQlQELerISGLTAEEAK--------EILLEK---VEEEARHEAAVLIKEIEE-EAKEE 185
|
170
....*....|....
gi 826320982 1323 EETKAKNALAHAVQ 1336
Cdd:PRK12704 186 ADKKAKEILAQAIQ 199
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1002-1096 |
4.37e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.61 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1002 QEAHQQTLDDLQAE-EDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDE 1080
Cdd:pfam11559 54 RESLNETIRTLEAEiERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAH 133
|
90
....*....|....*.
gi 826320982 1081 KLKKKEFEMSNLQSKI 1096
Cdd:pfam11559 134 EVKKRDREIEKLKERL 149
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
890-1042 |
4.59e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 890 QLQVQAEADSLADAEERCDQLIKT-KIQLEAKIKEATERAEDEEEINAELTakkrKLEDECSELKKDIDDLELTL-AKVE 967
Cdd:cd22656 95 EILELIDDLADATDDEELEEAKKTiKALLDDLLKEAKKYQDKAAKVVDKLT----DFENQTEKDQTALETLEKALkDLLT 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 826320982 968 KEKHATENK-VKNLTEEMAGLDENIAKLAKEKkalQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQ 1042
Cdd:cd22656 171 DEGGAIARKeIKDLQKELEKLNEEYAAKLKAK---IDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGP 243
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1167-1331 |
4.86e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.97 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1167 KKREAEFQKMRRDLEEATLQheATAAALRKKHADS-VAELGEQIDNLqrvkqkleKEKSELKMEiddlasnmETVSKAKG 1245
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH--------DVVLKKTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1246 NFEKMCRTLEDQLSEvktkeeeqqrLINELsaqkARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEET 1325
Cdd:pfam05911 82 EWEKIKAELEAKLVE----------TEQEL----LRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCE 147
|
....*.
gi 826320982 1326 KAKNAL 1331
Cdd:pfam05911 148 KEINSL 153
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1081-1248 |
5.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1081 KLKKKEFEMSNLQSKIEDEQAVGMQLQKKIKELQARTEELEEeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATS 1160
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKL--------RNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1161 AQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELgEQIDNLQR---VKQKLEKEKSELKMEIDDLASNM 1237
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLTAeeaKEILLEKVEEEARHEAAVLIKEI 178
|
170
....*....|.
gi 826320982 1238 ETVSKAKGNFE 1248
Cdd:PRK12704 179 EEEAKEEADKK 189
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
865-1585 |
5.10e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 865 LAKSEAKRKE-------LEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEATERAEDEEEINAE 937
Cdd:pfam10174 41 LKKERALRKEeaarisvLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 938 LTAKKRKLEDECSELKKDIDDLELtlaKVEKEKHATENKvknlteemaglDENIAKLakekkaLQEAHQQTLDDLQAEED 1017
Cdd:pfam10174 121 LQSEHERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESIKKL------LEMLQSKGLPKKSGEED 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1018 kvNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDL-ERAKRKLEgdlkLAQESTmdiendkqqldeklkkkefEMSNLQSKI 1096
Cdd:pfam10174 181 --WERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQ----LQPDPA-------------------KTKALQTVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1097 EDEQAVGMQLQKKIKELQarteeleEEIEAERAS-------------------------RAKAEKQRSDLSR---ELEEI 1148
Cdd:pfam10174 236 EMKDTKISSLERNIRDLE-------DEVQMLKTNgllhtedreeeikqmevykshskfmKNKIDQLKQELSKkesELLAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1149 SERLEEAGGATS---AQIEMNKKREAEfqkmrRDLEEATLQHEATAAALRKKHADSVaeLGEQIDNLQRvkqkLEKEKSE 1225
Cdd:pfam10174 309 QTKLETLTNQNSdckQHIEVLKESLTA-----KEQRAAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1226 LKMEIDDLASNMETVSKAKGNFEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEK----EALVS 1301
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKeriiERLKE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1302 QLSRGKQAFTQQIEELKRQLEEetkaknalahavqsARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDA 1381
Cdd:pfam10174 458 QREREDRERLEELESLKKENKD--------------LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1382 IHRTEELEEAKK-----KLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLA 1456
Cdd:pfam10174 524 IAVEQKKEECSKlenqlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1457 EWKhKYEETQAELEASQKESRSLSTELFKVKNAYEETLDQLETLKRENKNLQQEISDLTEqiaeggkhihELEKVKKQID 1536
Cdd:pfam10174 604 ELE-SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELD 672
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 826320982 1537 QEKSEL---QASLEEAEA---SLEHEEGKILRIQLELNQvkSEIDRKIAEKDEEI 1585
Cdd:pfam10174 673 ATKARLsstQQSLAEKDGhltNLRAERRKQLEEILEMKQ--EALLAAISEKDANI 725
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1298-1580 |
5.17e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.92 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1298 ALVSQLSRGKQAFTQQIEELKRQLEEE--TKAKNALAHAVQSARHDCDLLREQYEE------EQEAKAELQRGMSKANSE 1369
Cdd:NF033838 88 ALNKKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEatkkveEAEKKAKDQKEEDRRNYP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1370 VAQWRT----KYETDAIHRTEELEEAKKKL-----AQRLQDAEEHVEAVNSKCASLEKTK-QRLQNEVE-DLMIDVERSN 1438
Cdd:NF033838 168 TNTYKTleleIAESDVEVKKAELELVKEEAkeprdEEKIKQAKAKVESKKAEATRLEKIKtDREKAEEEaKRRADAKLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1439 AACIALDKKQRnfDKVLAEWKHKYEETQAELEASQKESRSLSTELfkvknaYEETLDQlETLKRENKnlqqeisdlteqI 1518
Cdd:NF033838 248 AVEKNVATSEQ--DKPKRRAKRGVLGEPATPDKKENDAKSSDSSV------GEETLPS-PSLKPEKK------------V 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 826320982 1519 AEGGKHIHELEKVKKQIDQEK----------------SELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAE 1580
Cdd:NF033838 307 AEAEKKVEEAKKKAKDQKEEDrrnyptntyktleleiAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE 384
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1780-1901 |
5.40e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1780 HLERMKKNMEQTVKDLQHRLDEAEQLAlkggKKQIQKLEARVRELENEVEgEQRRNVEAVKSLRKHERrvkeltyQTEED 1859
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH----EKQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES-------QSQED 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 826320982 1860 RKNvlRLQDLVDKLQtkvkAYKRQAEEAEEQSNVNLARFRKI 1901
Cdd:pfam15921 143 LRN--QLQNTVHELE----AAKCLKEDMLEDSNTQIEQLRKM 178
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
955-1057 |
5.80e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 955 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDENIAKLAKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVD 1034
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 826320982 1035 DLEGSLEQEKKLRMDLERAKRKL 1057
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
911-1113 |
6.46e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 911 IKTKIQLEaKIKEATERAED--------EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTE 982
Cdd:PRK05771 36 LKEELSNE-RLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 983 EMAGLDENIAKLAKEKKALQ--EAHQQTLDDLQAEED---KVNTLTKAKTKLEQQVDDLEGSLE-QEKKLRM-----DLE 1051
Cdd:PRK05771 108 EISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEYiSTDKGYVyvvvvVLK 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 826320982 1052 RAKRKLEGDLKLAQESTMDIENDKqQLDEKLKKKEFEMSNLQSKIEDeqavgmqLQKKIKEL 1113
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES-------LLEELKEL 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1538-1922 |
7.37e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1538 EKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIA-EKDEEID-QLKRNHLRVVESmqstldaeirsrndALR 1615
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSArESDLEQDyQAASDHLNLVQT--------------ALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1616 IKKKME---GDLNEMEIQLNHANRQASEAIRNLRNTQGVLKDTQLHLDDaIRSQ-DDLKEQLAMVERRANLMQAEV---E 1688
Cdd:COG3096 345 QQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS-LKSQlADYQQALDVQQTRAIQYQQAVqalE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1689 ELRASLEQTERSRKMAEQELLDASERVQLLHTqntSLINTKKKLE-TDISHIQGE-----MEDIVQE--ARNAEEKAKKA 1760
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQATE---EVLELEQKLSvADAARRQFEkayelVCKIAGEveRSQAWQTAREL 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1761 ITDAAMMAEELKKEQDTSAHLERMKKNMEQtvkdlQHRLDE-AEQLALKGGKK---------QIQKLEARVRELENEVE- 1829
Cdd:COG3096 501 LRRYRSQQALAQRLQQLRAQLAELEQRLRQ-----QQNAERlLEEFCQRIGQQldaaeeleeLLAELEAQLEELEEQAAe 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1830 -GEQRRNVEAvkSLRKHERRVKELTYQTEEDRKnvlrLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLARFRKIQHELEEA 1908
Cdd:COG3096 576 aVEQRSELRQ--QLEQLRARIKELAARAPAWLA----AQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDEL 649
|
410
....*....|....
gi 826320982 1909 EERADIAESQVNKL 1922
Cdd:COG3096 650 AARKQALESQIERL 663
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
920-1330 |
7.65e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 920 KIKEATERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKK 999
Cdd:COG5185 174 QNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1000 ALQEAHQQTlDDLQAEedkvntltkaktKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlAQESTMDIENDKQQLD 1079
Cdd:COG5185 254 KLEKLVEQN-TDLRLE------------KLGENAESSKRLNENANNLIKQFENTKEKIAEYTK-SIDIKKATESLEEQLA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1080 EKLKKKEFE--MSNLQSKIEDEQAVGMQLQKKIKELQARTEEleeeieaeRASRAKAEKQRSDLSRELEEISERLEEagg 1157
Cdd:COG5185 320 AAEAEQELEesKRETETGIQNLTAEIEQGQESLTENLEAIKE--------EIENIVGEVELSKSSEELDSFKDTIES--- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1158 atsaqiemnkKREaEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNM 1237
Cdd:COG5185 389 ----------TKE-SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREA 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1238 ETVSKAKGNFEKMCRTLEDQlSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQ-QIEE 1316
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVR-SKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRaRGYA 536
|
410
....*....|....
gi 826320982 1317 LKRQLEEETKAKNA 1330
Cdd:COG5185 537 HILALENLIPASEL 550
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
869-965 |
7.66e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.32 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 869 EAKRKELEEKMVTLMQEKNDLQLQVQAeadsLADAEERCDQLIKtkiQLEAKIKEATERAEDEEEINAELTAKKRKLEDE 948
Cdd:pfam13863 16 DAKREEIERLEELLKQREEELEKKEQE----LKEDLIKFDKFLK---ENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQ 88
|
90
....*....|....*..
gi 826320982 949 CSELKKDIDDLELTLAK 965
Cdd:pfam13863 89 IEELKSEISKLEEKLEE 105
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1255-1481 |
7.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1255 EDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEETKAKNALAHA 1334
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1335 VQSARHDCDLL---------------REQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAihrtEELEEAKKKLAQRL 1399
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKL----AELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1400 QDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSL 1479
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
..
gi 826320982 1480 ST 1481
Cdd:COG3883 251 AA 252
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1485-1598 |
9.38e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1485 KVKNAYEETLDQLETLKRENKNLQQEIsdlteqIAEGGKHIH----ELEKVKKQIDQEKSELQASLEEAEASLEHEEGKI 1560
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKKEA------LLEAKEEIHklrnEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 826320982 1561 LRIQLELNQVKSEIDRK---IAEKDEEIDQLKRNHLRVVES 1598
Cdd:PRK12704 106 EKREEELEKKEKELEQKqqeLEKKEEELEELIEEQLQELER 146
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1485-1651 |
9.40e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1485 KVKNAYEETLDQLETLKRENKNLQQEISDLTEQIaegGKHIHELEKVKKQIDQEKSELQASLEEAEASLEHEEGKilRIQ 1564
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKL---TDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEIK--DLQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1565 LELNQVKSEIDRKIAEKdeeIDQLKrnhlrvvesmqstldAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQASEAIRN 1644
Cdd:cd22656 186 KELEKLNEEYAAKLKAK---IDELK---------------ALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA 247
|
....*..
gi 826320982 1645 LRNTQGV 1651
Cdd:cd22656 248 LEKLQGA 254
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
939-1111 |
9.69e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 40.59 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 939 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLAKEKKALQeahqqtlddLQAEEDK 1018
Cdd:pfam15066 355 ITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKEKETLQ---------LELKKIK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1019 VNTL---TKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKR--KLEGDLKLAQESTMDIendkqqLDEKLKKKEFEMSNLQ 1093
Cdd:pfam15066 426 VNYVhlqERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERlqQLKGELEKATTSALDL------LKREKETREQEFLSLQ 499
|
170
....*....|....*...
gi 826320982 1094 SKIEDEQAVGMQLQKKIK 1111
Cdd:pfam15066 500 EEFQKHEKENLEERQKLK 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1686-1851 |
9.96e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1686 EVEELRASLEQTERSRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISHIQGEMEDIVQEARNAEEKAKKAITdaa 1765
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 826320982 1766 mmAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELENEVEGEQRRNVEAVKSLRKH 1845
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELE--------EELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*.
gi 826320982 1846 ERRVKE 1851
Cdd:COG1579 158 LEELEA 163
|
|
| |
